BIOCHEM – LECTURE

COVERAGE • Nerve cells are branched to conduct impulses from one

1. Cell point to another
2. Carbohydrates • Human WBCs can change their shape to engulf the
3. Proteins microorganisms enter the body.
4. Lipids Structure of Cell
- The detailed structure of a cell has been studied under
CELL compound microscope and electron microscope
- The basic structural and functional unit of living organisms. - Certain structures can be seen only under an electron
- Make up living things and carry out activities that keep a microscope.
living thing alive. - The structure of a cell as seen under an electron microscope
Cell Theory is called ultrastructure.
- A collection of ideas and conclusions from many different • Compound microscope – 2000x
scientists over time that describes cells and how cells • Electron microscope – 500,000x
operate. Animal Cell
1. Robert Hooke (1665) – discovered cell
2. Anton Van Leeuwenhoek (1674) – observed living cell
3. Robert Brown (1883) – discovered nucleus
4. Felix Dujardin (1835) – discovered fluid content of cell
5. Matthias Schleiden (1838) – proposed all plants are made
up of cells.
6. J.E. Purkinje (1839) – named fluid content of cell as
protoplasm.
Unicellular Organisms
- made up of only one cell
- Ex: Euglena, Paramecium, Yeast
Multicellular Organisms
- Made up of more than one cell
- Ex: Plants, animals, fungus

Size of Cells
- Most cells are very
small (microscopic),
some may be very large Plant Cell
(macroscopic)
- The unit used to
measure size of a cell is
micrometer
- 1 μm = 1/1000
millimeter

Shape of Cells
- Variation depends mainly upon the function of cells
- Some cells like euglena and Amoeba can change their shape,
but most cells have a fixed shape.
• Human RBCs are circular biconcave for easy passage
through human capillaries

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 BIOCHEM – LECTURE
Bacterial Cell
Structure of Cell
Plasma Membrane
- Extremely delicate, think, elastic, living and semi-
permeable membrane
- Made up of two layers of lipid molecules in which protein
molecules are floating
- Thickness varies from 75-110 A
- Can be observed under an electron microscope only
Functions:
• Maintain shape and size of the cell
• Protects internal contents
• Regulates entry and exit of substances in and out of the
cell
• Maintains homeostasis
Cell Wall
- Non-living and outermost covering of a cell (plants and
bacteria)
- Can be tough, rigid and sometimes flexible
- Made up of cellulose, hemicellulose and pectin
- May be thin or thick, multilayered structure
- Thickness varies from 50-1000 A
Functions:
• Provides definite shape, strength and rigidity
• Prevents drying up (desiccation) of cells
• Helps in controlling cell expansion
• Protects cell from external pathogens
Nucleus
- Dense spherical body located near the center of the cell
- Diameter varies from 10-25 μm
- Present in all the cells except red blood cells and sieve tube
cells
- Well developed in plant and animal cells
- Undeveloped in bacteria and blue-green algae
(cyanobacteria)
- Most of the cells are uninucleate (having only one nucleus)
- Nucleus has a double layered covering called nuclear
membrane
- Nuclear membrane has pores of diameter about 80-100 nm
- Colorless dense sap present inside the nucleus known as
nucleoplasm
- Nucleoplasm contains round shaped nucleolus and network
of chromatin fibers
- Fibers are composed of deoxyribonucleic acid (DNA) and
protein histone
- These fibers condense to form chromosomes during cell
division
- Chromosomes contain stretches of DNA called genes
- Genes transfer the hereditary information from one
generation to the next
Functions:
• Control all the cell activities like metabolism, protein
synthesis, growth and cell division
• Nucleolus synthesizes ribonucleic acid (RNA) to
constitute ribosomes
• Store hereditary Information In genes
Cytoplasm
- Jelly-like material formed by 80 % of water
- Present between the plasma membrane and the nucleus
- Contains a clear liquid portion called cytosol and various
particles
- Particles are proteins, carbohydrates, nucleic acids, lipids
and inorganic ions
- Also contains many organelles with distinct structure and
function
- Some of these organelles are visible only under an electron
microscope
- Granular and dense in animal cells and thin in plant cells
Endoplasmic Reticulum
- Network of tubular and vesicular structures which are
interconnected with one another
- Some parts are connected to the nuclear membrane, while
others are connected to the cell membrane
- Two types. Smooth (lacks ribosomes) and rough (studded
with ribosomes)
Functions
• Gives Internal support to the cytoplasm
• RER synthesize secretory proteins and membrane
proteins
• SER synthesize lipids for cell membrane
• In liver cells SER detoxify drugs & poisons
• In muscle cells SER store calcium Ions
Golgi body
- Discovered by Camillo Golgi
- Formed by stacks of S-8 membranous sacs
- Sacs are usually flattened and are called the cisternae
- Has two ends: cis face situated near the endoplasmic
reticulum and trans face situated near the cell membrane
Functions:
• Modifies, sorts and packs materials synthesized in the
cell
• Delivers synthesized materials to various targets Inside
the cell and outside the cell
• Produces vacuoles and secretory vesicles
• Forms plasma membrane and lysosomes
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 BIOCHEM – LECTURE
Lysosomes - They are found in storage organs such as fruits, tubers
- Small, spherical, single membrane sac and seeds.
- Found throughout the cytoplasm • Potato tubers - Food: Starch
- Filled with hydrolytic enzymes • Maize grains - Food: Protein
- Occur in most animal cells and in few types of plant cells • Castor seeds - Food: oil
Functions: Chloroplasts
• Help in digesting of large molecules - Double membrane-bound organelles found mainly in plant
• Protect cell by destroying foreign invaders like bacteria cells
and viruses - Usually spherical or discoidal in shape
• Degradation of worn-out organelles - Shows two distinct regions-grana and stroma
• In dead cells perform autolysis - Grana are stacks of thylakoids (membrane bound, flattened
discs)
Vacuoles
- Thylakoids contain chlorophyll molecules which are
- Single membrane sac filled with liquid of sap (water, sugar
responsible for photosynthesis
and ions) - Stroma is a colorless dense fluid
- In animal cells, vacuoles are temporary, small in size and Functions:
few in number • Convert light energy into chemical energy in the form
- In plant cells, vacuoles are large and more in number. of food
- May be contractile or non-contractile • Provide green color to leaves, stems and Vegetables
Functions: Centrosome
• Store various substances including waste products - Centrosome is the membrane bound organelle present near
• Maintain osmotic pressure of the cell the nucleus
• Store food particles in amoeba cells - Consists of two structures called centrioles
• Provide turgidity and rigidity to plant cells - Centrioles are hollow, cylindrical structures made of
Mitochondria microtubules
- Centrioles are arranged at right angles to each other
- Small, rod shaped organelles bounded by two membranes -
Functions:
inner and outer
• Form spindle fibers which help in the movement of
- Outer membrane Is smooth and encloses the contents of chromosomes during cell division
mitochondria • Help in the formation of cilia and flagella
- Inner membrane Is folded in the form of shelf like inward Cytoskeleton
projections called cristae - Formed by microtubules and microfilaments
- Inner cavity Is filled with matrix which contains many - Microtubules are hollow tubules made up of protein called
enzymes tubulin
- Contain their own DNA which are responsible for many - Microfilaments are rod shaped thin filaments made up of
enzymatic actions protein called actin
Functions: Functions:
• Synthesize energy rich compound ATP • Determine the shape of the cell
• ATP molecules provide energy for the vital activities of • Give structural strength to the cell
living cells • Responsible for cellular movements
Plastids
- double membrane-bound organelles found inside plants and Prokaryotic Cell Eukaryotic Cell
Nucleus is undeveloped Nucleus is well developed
some algae.
- They are responsible for activities related to making and Only one chromosome is More than one chromosome
present are present
storing food.
Membrane bound organelles Membrane bound organelles
- They often contain different types of pigments that can
are absent are present
change the color of the cell. Size ranges from 0.5-5 μm Size ranges from 5-100 μm
Chromoplasts Examples: Bacteria and blue Examples: All other
- produce and store pigments green algae organism
- They are responsible for different colors found in leaves,
fruits, flowers and vegetables. Animal Cell Plant Cell
• Carrot - Pigment: Carotene Generally small in size Generally large in size
• Mango - Pigment: Xanthophyll Cell wall is absent Cell wall is present
• Tomato - Pigment: Lycopene Plastids are absent Plastids are present
Leucoplasts Vacuoles are smaller in size Vacuoles are larger in size
- colorless plastids that store foods. and less in number and more in number
Centrioles are present Centrioles are absent
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 BIOCHEM – LECTURE
CARBOHYDRATES
Biochemical substance
- It is a chemical substance found within a living organism
- These substances are divided into two groups: bioinorganic
substances and bioorganic substances
- Human uses carbohydrates of the plat kingdom extend
beyond food
• Carbohydrates in the form of cotton and linens are
used as clothing
• Carbohydrates in the form of wood are used for
shelter and heating and in making paper
Occurrence and functions
• The most abundant class or bioorganic molecules on planet
earth
• In plants, it constitutes about 75% by mass of dry plant
materials
• Green (chlorophyll-containing) plants produce
carbohydrates via photosynthesis
• Plants have two main uses, the produce:
- Cellulose – serves as structural elements
- Starch – provide energy reserves
• Dietary intake of plant materials is the major carbohydrate
source for humans and animals
• The average human diet should ideally about two-thirds
carbohydrates by mass
Functions of Carbohydrates in Human
1. Oxidation provides energy
2. Storage, glycogen, provides a short-term every source
3. Supply carbon atoms for the synthesis of other biochemical
substances
4. Form part of the structural framework of DNA and RNA
molecules
5. Linked to lipids are structural components of cell
membranes
6. Linked to proteins function in a variety of cell-cell and cell-
molecule recognition process
Classification of Carbohydrates
- Most simple carbohydrates have empirical formula that fit the
general formula𝑪𝒏𝑯𝟐𝒏𝑶𝒏
- Early observation by scientists that the above-mentioned
formula can also be written as 𝑪𝒏􁈺𝑯𝟐𝑶􁈺𝒏 hydrate of water
- A polyhydroxy aldehyde, a polyhydroxy ketone or a
compound that yields polyhydroxy aldehydes or polyhydroxy
ketones upon hydrolysis
Monosaccharide
- Contains a single polyhydroxy aldehyde or polyhydroxy
ketone unit
- Cannot be broken down into simpler units by hydrolysis
(addition of water module)
- Pure monosaccharides are water-soluble, white, crystalline
solids
- Ex: Glucose and Fructose
Oligosaccharide
- Contains 2-10 monosaccharide units covalently bonded to
each other
- Disaccharide – most common type of oligosaccharide units
covalently bonded to each other
- Example: Sucrose (table sugar)
- Upon hydrolysis, oligosaccharides and polysaccharides
produce monosaccharide units
Polysaccharide
- Contains many monosaccharide units covalently bonded to
each other
- Ex: Cellulose, Starch
Chirality: Handedness in Molecules
Handedness
- An important general structure property of most
monosaccharide
- Two forms: left-handed and right-handed (mirror
images)
- This property in not restricted to carbohydrates
Mirror image
- The reflection of an objects in a mirror
a) Superimposable mirror image
- Coincide at all points when the image is laid upon
each other
- All are the same
b) Nonsuperimposable mirror image
- Not all points coincide when the images are laid
upon each other
- Exists in left-handed and right-handed
• Not all molecules possess handedness
• Any organic molecule that contains a carbon atom with four
different groups attached to it in a tetrahedral orientation
possesses handedness
• Chiral center – an atom in a molecule that has four different
groups tetrahedrally bonded to it
a) Chiral molecule – not superimposable
b) Achiral molecule – superimposable
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 BIOCHEM – LECTURE
Stereoisomerism: Enantiomers and Diastereomers
Stereoisomers
- Are isomeric molecules that have the same molecular
formula and sequence of bonded atoms but differ in three-
dimensional orientation of their atoms in space
Features that generate stereoisomerism:
• Presence of a chiral center in a molecule
• Presence of “structural rigidity” in a molecule
Enantiomers
Examples of Chiral Compound:
- Sometimes called optical isomers
- Molecules are nonsuperimposable mirror images of each
other
- Left and right-handed forms of a molecule with a single
chiral center are enantiomers
- Came from the Greek word “enantios” meaning opposite
Diastereomers
- Molecules are not mirror images of each other
- Ex: Cis-trans isomers of alkenes and cycloalkanes
- Molecules that contain more than one chiral center can also
exist in diastereomeric as well as enantiomeric forms

Not Chiral Compound:

Magkapareho un CH2, ang chiral

dapat magkakaiba un atoms.
ang tawag daw dyan ay Ethyl
Radical

hindi na siya tetrahedral (dapat apat

ung nakaattach sa carbon)
may doble bond siya

hindi siya chiral kasi cyclic compound

na tawag dito
Designating Handedness using Fischer Projection Formulas
• It is a two-dimensional structural
notation for showing the spatial
Basta ang chiral compound ay dapat tetrahedral (apat un naka-attach arrangement of groups about
sakanya) tapos dapat magkakaiba ung apat na atoms na nakaattach kay chiral centers in
carbon. molecules
• Chiral center is
represented as the
intersection of vertical
and horizontal lines
• The chiral center, which
is almost always
carbon, is not explicitly
shown

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 BIOCHEM – LECTURE
Interaction between chiral compounds
- Enantiomeric pair have the same interaction with achiral
molecules and different interactions with chiral
molecules
1. Enantiomers have identical:
• Boiling points
• Melting points
• Densities
• Intermolecular force strength
2. A pair of enantiomers have the same solubility in an achiral
solvent, such as ethanol, but differing solubilities in a chiral
solvent, such as D-2-Butanol
3. The rate and extent of reaction of enantiomers with another
reactant are the same if the reactant is achiral but differ if
the reactant is chiral
4. Receptor sites for molecules within the body have chirality
associated with them
Examples:
• Spearmint (D-Carvone) and Caraway (L-Carvone)
• D-Epinephrine (perfect fit with the cellular receptor)
and L-Epinephrine

Classification of Monosaccharide
- The term saccharide comes from the Latin word for sugar,
which is saccharum
- Only monosaccharide with 3-7 carbon atoms is commonly
found in nature
Aldose
Properties of Enantiomers - Monosaccharide that contains an aldehyde functional
• When plane-polarized light is passed through a solution group
containing a single enantiomer, the plane of the polarized - A polyhydroxy aldehyde
light is related counterclockwise (to the left) or clockwise Ketose
(to the right), depending on the enantiomer - A monosaccharide that contains a ketone functional group
• The extent of rotation depends on the concentration of the - A polyhydroxy ketone
enantiomer as well as on its identity - the term saccharide comes from the Latin word for “sugar”
• The two enantiomers of a pair rotate the plane-polarized which is saccharum
light the same number of degrees, but in opposite directions.
• Additional notations
- (+) means rotation to the right (clockwise)
- (-) means rotation to the left (counterclockwise)
• D-L configuration is not directly related to + and –
designations.
• D (+) – Mannose – right-handed isomer that rotates plane-
polarized light in a clockwise direction (to the right)
Optically Active Compound
- A compound that rotates the plane polarized light
- Achiral compound – are optically inactive
- Chiral molecules – optically active Biochemically important monosaccharide
Dextrorotatory compound D-Glyceraldehyde and Dihydroxyacetone
- Chiral compound that rotates the plane of polarized light in - The simplest of the monosaccharides
a clockwise direction - Are important intermediates in the process of glycolysis
Levorotatory compound
- Chiral compound that rotates the plane of polarized light in
a counterclockwise direction

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 BIOCHEM – LECTURE
D-Glucose
- Ripe fruits are a good source of glucose,
which is often referred to as grape sugar
- Other names are dextrose and blood sugar
- The normal glucose in human blood is in
the range of 70-100 mg/dL (1 dL = 100
mL)
- Cells use glucose as a primary source of
energy
D-Galactose
- D-Galactose and D-Glucose are epimers (C-4)
- Seldom encountered as a free monosaccharide
- In human body, it is synthesized from glucose in the
mammary glands for use in lactose (milk sugar), a
disaccharide consisting of a glucose unit and galactose unit
- Also called brain sugar because it a
component of glycoproteins (protein-
carbohydrate compounds) found in brain
and nerve tissue
- Also present in the chemical markers that
distinguish various types of blood – A, B,
AB, and O
D-Fructose
- Most important ketohexose
- Also known as levulose and fruit sugar
- The sweetest-tasting of all sugars
- Found in fruits and honey
- Sometimes used as dietary sugar
- Different in C-1 and C-2 with D-Glucose
D-Ribose
- An aldopentose
- A component of a variety of
complex molecules such as
RNA and ATP
- The compound 2 deoxy-D-
ribose is an important
component in nucleic acid
chemistry
Cyclic forms of Monosaccharides
• Experimental evidence indicates that for monosaccharides
containing five or more carbon atoms, such open-chain
structures are actually in equilibrium with two cyclic
structures, and the cyclic structures are the predominant
forms at equilibrium
Recall:
• Hemiacetals- both –OH and –OR groups are attached
to the same carbon atom
• Monosaccharides – the –OH and –OR groups are attached
to the carbonyl carbon
• The cyclic forms of monosaccharides result from the ability
of their carbonyl group to react intramolecularly with a
hydroxyl group
• Cyclization of glucose (hemiacetal) creates a new chiral
center at carbon 1, and the presence of this new chiral center
produce two stereoisomers, called α and β isomers
Pyranose
- Contains a six-atom ring
Furanose
- A five-atom ring
Reactions of Monosaccharides
1. Oxidation to acidic sugars
2. Reduction to sugar alcohols
3. Glycoside formation
4. Phosphate ester formation
5. Amino acid sugar formation
Oxidation to Acidic Sugars
- Monosaccharide oxidation can yield three different types of
acidic sugars depending on the oxidizing agent used
• Weak Oxidizing Agent
- Tollen’s and benedict Reagents
- Aldoses are converted into aldonic acid
• Aldoses are reducing sugars
- Reduces Ag to Ag in Tollen’s Reagent
- Reduces Cu to Cu in benedict reagent
• A reducing sugar is a carbohydrate that gives a positive test
with Tollen’s and Benedict’s solutions
• In basic conditions, ketoses also give positive results with
these reagents
• These tests are used to test glucose in the urine
• The color of the strip is compared with a chart to determine
the concentration of the glucose in the urine sample
• Strong oxidizing agent
- Oxidize both ends of a monosaccharide at the same time
to produce a dicarboxylic acid, aldaric acid
• In biochemistry systems, enzymes can oxidize the primary
alcohol end of an aldose to produce alduronic acid
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 BIOCHEM – LECTURE
Reduction to produce Sugar Alcohols Maltose
- The carbonyxl group can be reduced to a hydroxyl group - Often called malt sugar
using hydrogen as the reducing agent – sugar alcohols - Comes from the breakdown of starch common
D-Glucitol ingredient in baby foods and in malted sugar
- Common name is D-Sorbitol that is used as moisturizer - Made up 2 D-Glucose units
in foods and cosmetics - A reducing sugar
- Used as sweetening agent in chewing gum because it Cellobiose
cannot be used by bacteria as their food - Produced as an intermediate in the hydrolysis of the
Glycoside formation polysaccharide cellulose
- Reacting between monosaccharide and an alcohol - Like maltose, cellobiose two D-glucose units but has a
Glycoside β(1→4) glycosidic linkage
- Is an acetal formed from a cyclic monosaccharide by - Like maltose, cellobiose is a reducing sugar, has three
replacement of the hemiacetal carbon -OH group with isomeric forms in aqueous solution and upon hydrolysis
an – OR group produces two D-glucose molecules
Phosphate Ester Formation Lactose
- The hydroxyl group of a monosaccharide can react with - Made up of β-D-galactose
inorganic oxoacids to form inorganic esters. and a D-glucose unit
- Play important roles in the metabolism of carbohydrates joined by β(1→4)
Amino Sugar Formation glycosidic linkage
- One of the hydroxyl group is replaced with an amino group - Principal carbohydrate in
- The three common natural amino sugars: milk
- Human – 7% - 8% lactose
- Cow’s milk – 4%-5%
lactose
- Lactose intolerance: a condition in which people lack the
enzyme lactase needed to hydrolyze lactose to galactose and
glucose.
- Lactase hydrolyzes β(1-4) glycosidic linkages.
- Deficiency of lactase can be caused by a genetic defect,
• Amino sugars and their N-acetyl derivatives are important physiological decline with age, or by injuries to intestinal
building blocks of polysaccharides found in chitin and mucosa.
hyaluronic acid
• N-Acetyl-a-D-glucosamine and N-Acetyl-a-D- Polysaccharides
galactosamine - A polymer that contains many monosaccharide units bonded
- Are present in the biochemical markers on red blood to each other by glycosidic linkages
cells, which distinguish the various blood types - Polysaccharides are often also called glycans
Disaccharides 1. The identity of the monosaccharide repeating unit in the
- Has cyclic form can react with an alcohol to form a polymer chain
glycoside • Homopolysaccharide
- This is the same process in joining two or more • Heteropolysaccharide
monosaccharide units 2. The length of the polymer chain
- The most important chemical reaction of maltose is that of 3. The type of glycosidic linkage between monomer units
hydrolysis producing 2 D-glucose units 4. The degree of branching of the polymer chain
- Acidic condition is needed or maltase is needed
- If not treated, galactosemia can cause mental retardation in Storage polysaccharide
infants and even death. - a storage form for monosaccharides and is used as an energy
- Treatment involved exclusion of milk and milk products source in cells
from diet - to lower the osmotic pressure within cells
- The α form of lactose is sweeter to the taste and more - the most important storage polysaccharides are starch (in
soluble in water than the β form plant cells) and glycogen (in animal and human cells)
- The β form can be found in ice cream that has been stored - not sweet and don’t show positive tests with Tollen’s and
for a long time; its crystallizers and gives the ice cream a Benedict’s solutions whereas monosaccharides are sweet
gritty texture and show positive tests
- limited water solubility
Glycosidic Linkage - Examples:
- Is the bond in a disaccharide resulting from the reaction • Cellulose, starch in plants
between the hemiacetal carbon atom – OH • Glycogen in animals
- Always carbon-oxygen-carbon bond • chitin in arthropods

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 BIOCHEM – LECTURE
Starch • Chemical messenger lipids - steroid hormones and
- a storage form for monosaccharides and is used as an energy eicosanoids)
source in cells • Protective-coating lipids - biological waxes
- glucose is the monomeric unit a) Saponifiable lipids
- storage is the monomeric unit - contain esters, which can undergo saponification
- two types of polysaccharides isolated from starch: (hydrolysis under basic conditions) (waxes,
• Amylose: straight chain polymer – 15 -20% of the triglycerides, phosphoglycerides, sphingolipids)
starch and has α (1→4) glycosidic bonds
• Molecular mass: 50,000 (up to 1000 glucose units) • Simple lipids - contain two types of components (a fatty
Amylopectin acid and an alcohol)
- Branched chain polymer – 80 – 85% of the starch α(1→4) • Complex lipids - contain more than two components
glycosidic bond for straight chain and a (1→6) for branch (fatty acids, an alcohol, and other components)
- Molecular mass: 300,000 (up to 100,000 glucose units) – b) Nonsaponifiable lipids
higher than amylose - do not contain ester groups, and cannot be saponified
- Human can hydrolyze alpha linkage but not beta linkage (steroids, prostaglandins)
• Iodine is often used for the presence of starch in solution
• Starch-containing solutions turn a dark blue-black when
iodine is added
• As starch is broken down through acid or enzymatic
hydrolysis to glucose monomers, the blue-black color
disappears
Structural Polysaccharides
Cellulose
- Linear homopolysaccharide with β(1→4) glycosidic bond
- Up to 5000 glucose units with molecular mass of 900,000
amu
- Cotton is approximately 95% cellulose and wood are
approximately 50 cellulose that hydrolyzes β (1→4) linkage
so humans cannot digest cellulose
- Some animals have bacteria that produces cellulase in their Fatty Acids
guts in order for them to get free glucose from cellulose - long chain carboxylic acids
- In humans, it serves as dietary fiber in food – readily absorbs
water and results in softer stools and regular bowel
movement
- 23-35 g of dietary fiber is required everyday
Chitin
- Similar to cellulose in both function and structure
- Linear polymer with all β(1→4)glycosidic linkages – it has
a N-acetyl amino derivative of glucose
- Function is to give rigidity to the exoskeleton s of crabs,
lobsters, shrimp, insects and other arthropods

LIPIDS
- biological molecules that are insoluble in water but soluble
in nonpolar solvents.
- have a wider spectrum of compositions and structures Properties of Fatty acids:
because they are defined in terms of their physical properties
• The long, nonpolar hydrocarbon tails of fatty acids are
(water solubility).
responsible for most of the fatty or oily characteristics
- the waxy, greasy, or oily compounds found in plants and
of lipids.
animals.
• The carboxyl (COOH) group is hydrophilic under basic
- wax coating that protects plants
conditions, such as physiological pH (7.4):
- used as energy storage
- structural components (cell membranes)
- insulation against cold
Five Categories of Lipids:
• Energy-storage lipids - triacylglycerols
• Membrane lipids - phospholipids, sphingoglycolipids,
and cholesterol
• Emulsification lipids - bile acids
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 BIOCHEM – LECTURE
Micelles
- In aqueous solutions, fatty acids associate with each other in
spherical clusters
- which the hydrocarbon tails tangle each other up through
dispersion forces, leaving a “shell” of polar carboxylate ions
facing outwards, in contact with the water.
- Micelles are important in the transport of insoluble lipids in
the blood, and in the actions of soaps.
Characteristics of Fatty Acids:
• They are usually having straight chains (no branches) that
are about 10 to 20 carbon atoms in length.
• They usually have an even number of carbon atoms
(counting the carboxyl carbon).
• The carbon chains may be saturated (all single bonds) or
unsaturated (containing double bonds). Other than the
carboxyl group and the double bonds, there are usually no
other functional groups.
• Shorter fatty acids usually have lower
melting points than longer ones (stearic
acid [18C] = 700C, palmitic acid [16C]
= 630C).
• The double bonds are usually in cis
configurations:
Essential Fatty Acids:
- Fatty acids that must be obtained from dietary sources – are
not synthesized within the body
- Two most important essential fatty acids are:
• Linoleic acid (18:2) - omega 6
• Linolenic acid (18:3) - omega 3
- Both are needed for:
• Proper membrane structure
• Serve as starting materials for the
production of several nutritionally
important longer-chain omega-6 and
omega-3 fatty acids
- In the body, they are used to produce hormonelike
substances that regulate blood pressure, blood clotting,
blood lipid levels, the immune response, and inflammatory
reactions.
Types of Fatty Acids
Saturated vs Unsaturated fatty acid
- The cis-double bonds in unsaturated fatty acids put an
inflexible “kink” in the carbon chain, preventing the
molecules from packing together as tightly as saturated fatty
acids do.
- For example, stearic acid (saturated), oleic acid (one double
bond), and linoleic acid (two double bonds) all have 18
carbons in the chain, but their melting points are drastically
different:
- Carboxylic acids with linear (unbranched) carbon chain -
Fatty acids are naturally occuring monocarboxylic acids
- Even number of Carbon atoms:
o Long chain fatty acids: C12 - C26
o Medium chain fatty acids: C6 - C11
o Short-chain fatty acids: C4 - C5
- Two Types:
o Saturated - all C-C bonds are single bonds
o Unsaturated
o Monounsaturated: one C=C bond
o Polyunsaturated: 2 or more C=C bonds present - up
to six double bonds are present in fatty acids
Saturated Fatty Acids
– Numbering starts from the end of -COOH group
– See structural notation: it indicates number of C atoms
– Example - Lauric acid has 12 C atoms and no double bonds
so it is (12:0)
Unsaturated Fatty Acids
– A monounsaturated fatty acid is a fatty acid with a carbon
chain in which one carbon–carbon double bond is present.
– Different ways of depicting the structure
– Selected Unsaturated Fatty Acids of Biological Importance
• Numbering starts from the other end of COOH
• See structural notation: it indicates number of C atoms
• E.g., 18:2 – 18 carbons, 2 double bonds
Polyunsaturated Fatty Acid (PUFAs)
- a fatty acid with a carbon chain in which two or more
carbon–carbon double bonds are present.
– Up to six double bonds are found in biochemically important
PUFAs.
– Two types of unsaturated fatty acids.
• Omega (ω)-3 fatty acids - An unsaturated fatty acid
with its endmost double bond three carbon atoms away
from its methyl end.
• Omega(ω)-6 fatty acid is an unsaturated fatty acid with
its endmost double bond six carbon atoms away from
its methyl end.
Omega Acids
– Essential Fatty Acids: Must be part of diet
– Nutritionally important Omega-3 and Omega-6 fatty acids
• Linolenic acid – Omega-3
• Linoleic acid – Omega-6
– Linoleic Acid Deficiency:
• Skin redness - becomes irritated
• Infections and dehydration
• Liver abnormalities
• Children need it the most
• Human milk has more than cow’s milk
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 BIOCHEM – LECTURE
American Diet
– Sufficient in omega 6 fatty acids
– Deficient in omega 3 fatty acids
• Fish - good source for omega 3 fatty acids
– High rate of heart disease may be due to imbalance in omega
3 and 6 fatty acids
• Ideal ratio: Omega 6: Omega 3 (4 - 10 g: 1g)
Physical Properties of Fatty Acids
– Water solubility: Short chain fatty acids have some
solubility whereas long chain fatty acids are insoluble
• Short chain fatty acids are sparingly soluble because
of carboxylic acid polar group
– Physical properties such as melting point depends on the
number of C atoms and degree unsaturation
The Melting Point
– Melting Point Depends Upon:
• Length of carbon chain
• Degree of unsaturation (number of double bonds in a
molecule)
Space Filling Molecules
- The number of bends in a fatty acid chain increase as the
number of double bonds increase
• Less packing occurs
• Melting point is lower
• Tend to be liquids at room temperature
Energy- Storage Lipids: Triacylglycerol’s
- With the notable exception of nerve cells, human cells store
small amounts of energy providing materials:
• The most widespread energy storage material -
carbohydrate glycogen
• Present in small amounts
- Storage material is the triacylglycerols:
• Triacylglycerols are concentrated primarily in special
cells (adipocytes)
• Nearly filled with the material.
Two Types of Triacylglycerols:
1) Simple Triacylglycerols: Three identical fatty acids are
esterified
Naturally occurring simple triacylglycerols are rare
2) Mixed Triacylglycerols: A triester formed from the
esterification of glycerol with more than one kind of fatty
acid
In nature mostly mixed triacylglycerols are found and
are different even from the same source depending on
the feed,
e.g., corn, peanut and wheat -fed cows have different
triacylglycerols
Fats and Oils
- Animal fats and vegetable oils are esters composed of three
molecules of a fatty acid connected to a glycerol molecule,
producing a structure called a triglyceride or triacylglycerol
The fatty acids in a triglyceride molecule are usually not all the
same natural triglycerides are often mixtures of many different
triglyceride molecules.
• Fats are triglycerides that are solids at room temp.
- usually derived from animals
- mostly saturated fatty acids
• Oils are triglycerides that are liquids at room temp.
- usually derived from plants or fish
- mostly unsaturated fatty acids
Chemical Properties of Fats and Oils:
• Triglycerides can be broken apart with water and an acid
catalyst (hydrolysis), or by digestive enzymes called lipases
“Good Fats” Versus “Bad Fats”
Current recommended amounts are: total fat intake in
calories:
• 15% - Monounsaturated fat
• 10% - Polyunsaturated
• <10% - Saturated fats
Saturated fats are considered “bad fats”
Monounsaturated fats are considered “good fats”
Trans-monounsaturated fats are considered “bad fats”
Polyunsaturated fats can be both “good fats” and “bad fats”
• Omega 3 and 6 are important “good fats”
Fat and Fatty Acid Composition of Nuts
- Numerous studies now indicate that eating nuts can have a
strong protective effect against coronary heart disease:
• Low amounts of saturated fatty acids
• Nuts also contain valuable antioxidant vitamins,
minerals, and plant fiber protein
Chemical Reactions of Triacylglycerols
Partial Hydrolysis
- Chemical Properties due to two functional groups: esters
and alkenes
• Hydrolysis: Partial hydrolysis of triacylglycerols
• Breaking of 1-2 ester bonds to give rise to mono- or
diacylglycerol and fatty acid(s)
• Carried out by enzymes produced by the pancreas
Saponification
- Triglycerides react with strong bases (NaOH or KOH) to
form the carboxylate salts of the fatty acids called soaps
- Hydrolysis in basic solution: Produce salt of fatty acid and
glycerol
- RCOOR’ + NaOH → RCOONa (soap) + R’OH
Soaps
- NaOH produces a “hard” soap, commonly found in bar
soaps; KOH produces a “soft” soap, such as those in shaving
creams and liquid soaps.
- These salts combine two solubility characteristics:
1) a long, nonpolar, water-insoluble (hydrophobic)
hydrocarbon “tail.”
2) charged, water-soluble (hydrophilic) “head.”
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 BIOCHEM – LECTURE
- In water, the “tails” become tangled, leaving the charged
heads sticking out into the solution, forming a structure
called a micelle.
Hydrogenation
- alkenes are converted into alkanes with hydrogen gas
(H2) and a catalyst (Pt, Ni, or some other metal).
- used to convert unsaturated vegetable oils, which are
liquids at room temp., to saturated fats, which are
solids at room temp. (shortening, etc.).
- In partially hydrogenated vegetable oils, not all of the
double bonds are saturated, allowing the texture of the
product to be controlled.
- In the process, this twists some of the naturally-
occurring cis double bonds into trans isomers (trans
fats).
• Addition of hydrogen across double (=) bond -
increases degree of saturation
• Many food products are produced by partial
hydrogenation of oils and fats
• Peanut oil + H2 → Peanut Butter
• Vegetable oil + H2 → Margerine
O phosphate group, a platform molecule (glycerol or
O
H2 C O C
H2 C O C
O O
HC O C + 2H2 HC O C
O O
H2 C O C
H2 C O C
Oil Solid
Oxidation
- Double bonds in triacylglycerols are subject to
oxidation with oxygen in air (an oxidizing agent)-
Leads to C=C breakage
- oxidation of alkenes may result into two short chain
molecules – an aldehyde or a carboxylic acid:
- The aldehydes and/or carboxylic acids so produced
often have objectionable odors - fats and oils are said
to be rancid
- To avoid this unwanted oxidation process antioxidants
are added as preservatives, e.g., Vitamin C and vitamin
E are good antioxidant preservatives.
Waxes
- simple lipids contain a fatty acid joined to a long-chain (12-
32 carbons) alcohol
- insoluble in water, and not as easily hydrolyzed as fats and
oils. They often occur in nature as protective coatings on
feathers, fur, skin, leaves, and fruits.
- Sebum, secreted by the sebaceous glands of the skin,
contains waxes that help to keep skin soft and prevent
dehydration.
- used commercially to make cosmetics, candles, ointments,
and protective polishes.
Membrane Lipids: Phospholipids
– All cells are surrounded by a membrane that confines their
contents.
– Up to 80% of the mass of a cell membrane can be lipid
materials and these lipid materials are dominated by
phospholipids.
– A phospholipid contains one or more fatty acids, a
sphingosine) to which the fatty acid(s) and the phosphate
group are attached, and an alcohol that is attached to the
phosphate group.
Glycerophospholipids
– a lipid that contains two fatty acids and a phosphate group
esterified to a glycerol molecule and an alcohol esterified to
the phosphate group.
– All attachments (bonds) between groups in a
glycerophospholipid are ester linkages
– have four ester linkages as contrasted to three ester linkages
in triacylglycerols.
– undergo hydrolysis and saponification reactions in a manner
similar to that for triacylglycerols
– The alcohol attached to the phosphate group in a
glycophospholipid is usually one of three amino alcohols:
choline, ethanolamine, or serine - respectively known as
phosphatidylcholines, phosphatidylethanolamines, and
phosphatidylserines.
– Structurally glycerophospholipids are alghough similar to
triacylglycerols, they have different biochemical functions.
• Triacylglycerols serve as energy storage molecules
• Glycerophospholipids function as components of
cell membranes
- A major structural difference between the two types of lipids
is that of their “polarity” – Responsible for their differing
biochemical functions.
• Triacylglycerols are a non-polar
• Glycerophospholipids are polar.
Sphingophospholipids
– Structures based on the 18-carbon monounsaturated
aminodialcohol sphingosine
– contains one fatty acid and one phosphate group attached to
a sphingosine molecule and an alcohol attached to the
phosphate group
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Saponifiable lipids
– which the alcohol esterified to the phosphate group is
choline are called sphingomyelins.
Sphingomyelins
– are found in all cell membranes and are important
structural components of the myelin sheath of neurons
• Sphingoglycolipids: Contains both a fatty acid and
carbohydrate
• Simple sphingoglycolipids are called cerebrosides: contains
a single monosaccharide unit - either glucose or galactose
– They occur primarily in brain (7% of dry mass)
Gangliosides
- Complex sphingoglycolipids
- contain a branched chain of up to seven monosaccharide
residues.
- Occur in the gray matter of the brain as well as in the myelin
sheath.
Membrane Lipids: Cholesterol
- the most abundant steroid in the body.
- It is an essential component of cell membranes, and is a
precursor for other steroids, such as the bile salts, sex
hormones, vitamin D, and the adrenocorticoid hormones.
- There is apparently a correlation between high levels of
cholesterol in the blood and atherosclerosis.
Cholesterol-Third major type of membrane lipid:
- Lipids: Fused Rings
- Cholesterol: C27 steroid molecule
- A steroid is a lipid whose structure is based on a fused ring
system of three 6 carbon rings and one 5 carbon ring.
- Important in human cell membranes, nerve tissue and brain
tissue
- Important in chemical synthesis: Hormones, vitamins
essential for life
Cholesterol in Food:
• Liver synthesizes cholesterol: ~ 1g everyday; so it is not
necessary to consume in the form of diet
• Cholesterol synthesis decrease if it is ingested but
reduction is not sufficient: Leads to cardiovascular disease
• Animal Food: Lot of cholesterol
• Plant Food: No cholesterol
Phosphoglycerides
- complex lipids that are major components of cell
membranes.
- Phosphoglycerides and related compounds are also called
phospholipids.
Amino alcohols in Phosphoglycerides
- The most abundant phosphoglycerides contain the alcohols
choline, ethanolamine, or serine attached to the phosphate
group
Lecithin
- Phosphoglycerides that contains the aminoalcohol choline
- The fatty acids at the first and second positions are variable,
so there are a number of different possible lecithins.
- Because lecithin’s contain negatively charged oxygen atoms
in the phosphate group and positively charged nitrogen
atoms in the quaternary ammonium salt group, that end of
the molecule is highly hydrophilic, while the rest of the
molecule is hydrophobic.
• This allows lecithin to act as an emulsifying agent:
- forms an important structural component of cell
membranes.
- forms micelles which play a role in the transport of
lipids in the blood stream.
- Commercially, lecithin extracted from soybeans is
used as an emulsifying agent in margarine and candies
to provide a smooth texture.
Cephalins
- Phosphoglycerides that contains the aminoalcohols
ethanolamine or serine
- found in most cell membranes, and are particularly abundant
in brain tissue. They are also found in blood platelets, and
play a role in blood clotting.
Sphingolipids
- complex lipids that contain sphingosine instead of glycerol.
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Sphingomyelins
- have sphingosine or a related dihydroxyamine as their
backbone
- abundant in brain and nerve tissue
- major constituent of the coating around nerve fibers
Glycolipids
- sphingolipids that contain carbohydrates (usually
monosaccharides).
- They are also referred to as cerebrosides because of their
abundance in brain tissue.
Biological Membranes
- Most cell membranes contain about 60% lipids and 40%
proteins:
• phosphoglycerides (e.g., lecithin and cephalin)
• sphingomyelin
• cholesterol
- The fluid-mosaic model of the cell pictures the cell
membrane as being composed of a lipid bilayer, in which
the nonpolar tails of lipids point towards the “interior” of the
bilayer, leaving the polar, hydrophilic portions pointing
outwards.
- When the membrane is broken, the repulsion between the
nonpolar portion and water causes the membrane to re-form.
• Cell membranes also contain unsaturated fatty acid
chains that increase the flexibility or fluidity of the
membrane.
• Some of the proteins in the membrane “float” in the
lipid bilayer like icebergs, while others extend through
the bilayer.
• The lipid molecules are free to move laterally within
the bilayer like dancers on a crowded dance floor.
Fluid Mosaic Model
- lipids of the bilayer are in constant motion, gliding from one
part of their bilayer to another at high speed
Bile Salts
- yellowish brown or green fluid produced in the liver and - classified as lipids because they are soluble in nonpolar
stored in the gall bladder.
- act like soaps and other emulsifiers: they contain both polar
and nonpolar regions, helping to break fats in foods into - The basic steroid structure contains four fused rings
smaller pieces, allowing them to be hydrolyzed more easily.
Gallstones
- Bile salts also emulsify cholesterol in the bile, so it can be
removed in the small intestine.
- If cholesterol levels are too high or the levels of bile salts is - Classified into three major groups:
too low, the cholesterol precipitates and forms gallstones.
- Gallstones can block the duct that allows bile to be secreted
into the duodenum.
- Fats are no longer digested properly, and bile pigments
absorbed into the blood causes the skin to become yellow
and the stool to become gray.
Prostaglandins
- cyclic compounds synthesized from arachidonic acid.
- Like hormones, they are involved in a host of body
processes, including reproduction, blood clotting,
inflammation, and fever. (Aspirin works by inhibiting
prostaglandin production, alleviating inflammation and
fever. NSAIDs has the similar mechanism)
Emulsification Lipids: Bile Acids
– An emulsifier is a substance that can disperse and stabilize
water-insoluble substances as colloidal particles in an
aqueous solution.
– Bile Acids: Cholesterol derivatives that functions as
emulsifying agents that make dietary lipids soluble in
aqueous environment of the digestive tract:
• Approximately one third of cholesterol produced by
liver is converted to bile acids.
• Action similar to soap in washing
Bile Acids
– tri- or dihydroxy cholesterol derivatives
– The carbon 17 side chain of cholesterol has been oxidized to
a carboxylic acid
– The oxidized acid side chain is bonded to an amino acid
(either glycine or taurine) through an amide linkage
– Bile is a fluid containing emulsifying agents (Bile acids)
secreted by the liver, stored in the gallbladder, and released
into the small intestine during digestion
Messenger Lipids: Steroid Hormones
- A hormone is a biochemical substance produced by a
ductless gland that has a messenger function.
- Hormones serve as a means of communication between
various tissues.
• Some hormones are lipids.
- The lipids that play the role of “chemical messengers”
include:
• Steroid hormones – derivatives of cholesterol
• Eicosanoids- derivatives of arachidonic acid
- There are two major classes of steroid hormones:
• Sex hormones - control reproduction and secondary
sex characteristics
• Adrenocorticoid hormones – control numerous
biochemical processes in the body
Steroids
solvents, but they are nonsaponifiable because the
components are not held together by ester linkages.
Sex hormones
- produced in the testes and ovaries regulate the production of
sperm and eggs and aid in the development of secondary sex
characteristics.
• Estrogens - the female sex hormones
• Androgens - the male sex hormones
• Progestins - the pregnancy hormones
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Adrenocorticoid hormones
- Hormones are chemicals released by cells or glands in one part
of the body that send out messages that affect cells in other
parts of the body. Many hormones are based on steroids.
- 28 Different hormones have been isolated from the adrenal
cortex
- are produced in the adrenal glands (located on the top of the
kidney).
- Two types of adrenocorticoid hormones:
• Glucocorticoids
- control glucose metabolism and counteract
inflammation
- such as cortisol affect the metabolism of
carbohydrates.
- Cortisol and its derivatives, cortisone and
prednisolone (synthetic) are powerful anti-
inflammatory drugs used to treat arthritis and asthma.
• Mineralocorticoids
- control the balance of Na and K ions in cells
- regulate ion concentration (mainly Na+).
- Aldosterone influces the absorption of Na+ and Clin
kidney tubules, thus regulating the retention of water
in the body
Messenger Lipids: Eicosanoids
• Eicosanoids Arachidonic acid (20:4) derivatives:
Have profound physiological effects at extremely low
concentrations.
Eicosanoids are hormone-like molecules
Exert their effects in the tissues where they are
synthesized.
Eicosanoids usually have a very short “life.”
Physiological effects of eicosanoids:
• Inflammatory response
• Production of pain and fever
• Regulation of blood pressure
• Induction of blood clotting
• Control of reproductive functions, such as
induction of labor
• Regulation of the sleep/wake cycle
Three Types
1. Prostoglandins:
- C20-fatty-acid derivative containing cyclopentane ring
and oxygen-containing functional groups
- Involved in raising body temperature,
- Inhibiting the secretion of gastric juices,
- Increasing the secretion of a protective mucus layer into
the stomach,
- Relaxing and contracting smooth muscle, directing
water and electrolyte balance, intensifying pain, and
enhancing inflammation responses.
2. Thromboxanes:
- C20-fatty-acid derivative containing a cyclic ether ring
and oxygen-containing functional groups
- Promote platelet aggregation.
3. Leukotrienes:
- C20-fatty-acid derivative containing three conjugated
double bonds and hydroxy groups
- Promote inflammatory and hypersensitivity (allergy)
responses
Protective- Coating Lipids: Biological Waxes
– A biological wax: a monoester of a long-chain fatty acid and
a long-chain alcohol.
– The fatty acids found in biological waxes:
• Generally are saturated fatty acids
• Contain 14 to 36 carbon atoms.
– The alcohols found in biological waxes:
• May be saturated or unsaturated
• May contain 16 to 30 carbon atoms.
Properties of Biological waxes:
- Water-insoluble and water-repellent because of long
nonpolar hydrocarbon chains.
- Humans and animals secrete biological waxes from
skin glands
Function of biological waxes:
– Protect hair and skin; and keep it pliable and lubricated.
– Impart water repellency to animal fur.
– Birds keep their feathers water repellent and help
minimize loss of body heat
– Plants coat their leaves with a thin layer of biological
waxes to prevent excessive evaporation of water and to
protect against parasite attack.
PROTEINS
- Greek proteios, “primary” or “of first importance”
- biochemical molecules consisting of polypeptides joined by
peptide bonds between the amino and carboxyl groups of
amino acid residues.
- Proteins perform a number of vital functions:
• Enzymes are proteins that act as biochemical
catalysts.
• Many proteins have structural or mechanical
functions (e.g., actin and myosin in muscles).
• Proteins are important in cell signaling, immune
responses, cell adhesion, and the cell cycle.
• Proteins are a necessary component in animal diets.
- All proteins are polymers containing chains of amino acids
chemically bound by amide (peptide) bonds.
- Most organisms use 20 naturally-occurring amino acids to
build proteins. The linear sequence of the amino acids in a
protein is dictated by the sequence of the nucleotides in an
organisms’ genetic code.
- These amino acids are called alpha (a)-amino acids because
the amino group is attached to the first carbon in the chain
connected to the carboxyl carbon.
Amino Acids
- classified by the polarity of the R group side chains, and
whether they are acidic or basic:
• neutral, nonpolar
• neutral, polar
• basic, polar (contains an additional amino group)
• acidic, polar (contains an additional carboxylate group)
- All of the amino acids are also known by a three letter and
one-letter abbreviations.
- Since the amino acids (except for glycine) contain four
different groups connected to the a-carbon, they are chiral,
and exist in two enantiomeric forms:
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 BIOCHEM – LECTURE
- The amino acids in living systems exist primarily in the L
form.
- Because amino acids contain both an acidic and a basic
functional group, an internal acid-base reaction occurs,
forming an ion with both a positive and a negative charge
called a zwitterion:
- In solution, the structure of an amino acid can change with
the pH of the solution
- In solution, the structure of an amino acid can change with
the pH of the solution.
Amino acids: Zwitterions
- Lowering the pH of the solution causes the zwitterion to
pick up a proton:
- Increasing the pH of the solution causes the zwitterion to
lose a proton:
- Since the pH of the solution affects the charge on the amino
acid, at some pH, the amino acid will form a zwitterion. This
is called the isoelectric point.
- Each amino acid (and protein) has a characteristic isoelectric
point:
- those with neutral R groups are near a pH of 6, those with
basic R groups have higher values, and those with acidic R
groups have lower values.
- Because amino acids can react with both H3O+ and OH-,
solutions of amino acids and proteins can act as buffers.
(E.g., blood proteins help to regulate the pH of blood.)
Reaction of Amino acids: Oxidation
- Amino acids can undergo any of the reaction’s characteristic
of the functional groups in the structure.
- Cysteine is the only amino acid that contains a sulfhydryl
(thiol, R—SH) group. Thiols are easily oxidized to form
disulfide bonds (R—S—S—R). This allows cysteine to
dimerize to form cystine
Peptide formation
- Amides can be thought of as forming from the reaction of
an amine and a carboxylic acid:
- In the same way, two amino acids can combine to form a
dipeptide, held together by a peptide bond:
Peptides
- Short chains are referred to as peptides, chains of up to about
50 amino acids are polypeptides, and chains of more than 50
amino acids are proteins. (The terms protein and
polypeptide are often used interchangeably.)
- Amino acids in peptide chains are called amino acid residues.
• The residue with a free amino group is called the N-
terminal residue, and is written on the left end of the
chain.
• The residue with a free carboxylate group is called the
C-terminal residue, and is written on the right end of the
chain.
- Peptides are named by starting at the N-terminal end and
listing the amino acid residues from left to right.
- Large amino acid chains are unwieldy to draw in their
complete forms, so they are usually represented by their
three-letter abbreviations, separated by dashes:
• Gly-Ala (Gly = N-terminal, Ala = C-terminal)
• Ala-Gly (Ala = N-terminal, Gly = C-terminal)
- The tripeptide alanylglycylvaline can be written as Ala-Gly-
Val. (There are five other arrangements of these amino acids
that are possible.)
- Insulin has 51 amino acids, with 1.55x1066 different
possible arrangements, but the body produces only one.
Oxytocin and Vasopressin
- More than 200 peptides have been identified as being
essential to the body’s proper functioning.
- Vasopressin and oxytocin are nonapeptide hormones
secreted by the pituitary gland. Six of the amino acid
residues are held in a loop by disulfide bridges formed by
the oxidation of two cysteine residues.
• Even though the molecules are very similar, their
biological functions are quite different:
• Vassopressin is known as antidiuretic hormone (ADH)
because it reduces the amount of urine formed, which
causes the body to conserve water. It also raises blood
pressure.
• Oxytocin causes the smooth muscles of the uterus to
contract, and is administered to induce labor. It also
stimulates the smooth muscles of mammary glands to
stimulate milk ejection.
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 BIOCHEM – LECTURE
Adrenocorticotropic hormone
- 39-residue peptide produced in the pituitary gland.
- It regulates the production of steroid hormones in the cortex
of the adrenal gland.
Characteristics of Proteins: Size
- Proteins are very large polymers of amino acids with
molecular weights that vary from 6000 amu to several
million amu.
• Glucose (C6H12O6 ) = 180 amu
• Hemoglobin (C2952H4664O832N812S8Fe4) = 65,000
amu
- Proteins are too large to pass through cell membranes, and
are contained within the cells where they were formed
unless the cell is damaged by disease or trauma.
• Persistent large amounts of protein in the urine are
indicative of damaged kidney cells.
• Heart attacks can also be confirmed by the presence of
certain proteins in the blood that are normally confined
to cells in heart tissue.
Acid Base Properties of Proteins
- Proteins take the form of zwitterions. They have
characteristic isoelectric points, and can behave as buffers
in solutions.
- The tendency for large molecules to remain in solution or
form stable colloidal dispersions depends on the repulsive
forces acting between molecules with like charges on their
surfaces.
• When proteins are at a pH in which there is a net
positive or negative charge, the like charges cause the
molecules to repel one another, and they remain
dispersed.
• When the pH is near the isoelectric point, the net charge
on the molecule is zero, and the repulsion between
proteins is small. This causes the protein molecules to
clump and precipitate from solution.
Protein Function
- Proteins perform crucial roles in all biological processes.
1. Catalytic function: Nearly all reactions in living organisms
are catalyzed by proteins functioning as enzymes. Without
these catalysts, biological reactions would proceed much
more slowly.
2. Structural function: In animals structural materials other
than inorganic components of the skeleton are proteins, such
as collagen (mechanical strength of skin and bone) and
keratin (hair, skin, fingernails).
3. Storage function: Some proteins provide a way to store
small molecules or ions, e.g., ovalbumin (used by embryos
developing in bird eggs), casein (a milk protein) and gliadin
(wheat seeds), and ferritin (a liver protein which complexes
with iron ions).
4. Protective function: Antibodies are proteins that protect the
body from disease by combining with and destroying
viruses, bacteria, and other foreign substances. Another
protective function is blood clotting, carried out by thrombin
and fibrinogen.
5. Regulatory function: Body processes regulated by proteins
include growth (growth hormone) and thyroid functions
(thyrotropin).
6. Nerve impulse transmission: Some proteins act as
receptors for small molecules that transmit impulses across
the synapses that separate nerve cells (e.g., rhodopsin in
vision).
7. Movement function: The proteins actin and myosin are
important in muscle activity, regulating the contraction of
muscle fibers.
8. Transport function: Some proteins bind small molecules
or ions and transport them through the body.
• Serum albumin is a blood protein that carries fatty acids
between fat (adipose) tissue and other organs.
• Hemoglobin carries oxygen from the lungs to other
body tissues.
• Transferrin is a carrier of iron in blood plasma.
• A typical human cell contains 9000 different proteins;
the human body contains about 100,000 different
proteins.
Protein Classes by Structure
- Proteins can be classified on the basis of their structural
shapes:
- Fibrous proteins are made up of long rod-shaped or
stringlike molecules that can intertwine with one another
and form strong fibers.
• insoluble in water major components of connective
tissue, elastic tissue, hair, and skin e.g., collagen,
elastin, and keratin.
- Globular proteins are more spherical in shape
• dissolve in water or form stable suspensions.
• not found in structural tissue but are transport proteins,
or proteins that may be moved easily through the body
by the circulatory system
• e.g., hemoglobin and transferrin.
Protein Classes by Composition
Proteins can also be classified by composition:
• Simple proteins contain only amino acid residues.
• Conjugated proteins also contain other organic or
inorganic components, called prosthetic groups.
a) nucleoproteins — nucleic acids (viruses).
b) lipoproteins — lipids (fibrin in blood, serum
lipoproteins)
c) glycoproteins — carbohydrates (gamma globulin in
blood, mucin in saliva)
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 BIOCHEM – LECTURE
d) phosphoproteins — phosphate groups (casein in milk)
e) hemoproteins — heme (hemoglobin, myoglobin,
cytochromes)
f) metalloproteins — iron (feritin, hemoglobin) or zinc
(alcohol dehydrogenase)
Protein Structure
- The structure of proteins is much more complex than that of
simple organic molecules.
- Many protein molecules consist of a chain of amino acids
twisted and folded into a complex three-dimensional
structure
- The complex 3D structures of proteins impart unique
features to proteins that allow them to function in diverse
ways.
- There are four levels of organization in proteins structure:
primary, secondary, tertiary, and quaternary.
Primary structure
- The linear sequence of the side chains that are connected
to the protein backbone
- Each protein has a unique sequence of amino acid
residues that cause it to fold into a distinctive shape that
allows the protein to function properly
Secondary Structure
- Hydrogen bonding causes protein chains to fold and align to
produce orderly patterns called secondary structures.
The a-Helix
- a single protein chain twisted to resemble a coiled helical
spring.
- held in this shape by hydrogen bonding interactions between
amide groups, with the side chains extending outward from
the coil.
- The amount of a-helix coiling in proteins is highly variable.
- In a-keratin (hair, pictured below), myosin (muscles),
epidermin (skin), and fibrin (blood clots), two or more
helices coil together (supracoiling) to form cables.
The b-Pleated Sheet
- Another secondary structure is the b-pleated sheet, in which
several protein chains lie side by side, held by hydrogen
bonds between adjacent chains less common than the a-
helix;
- it is found extensively only in the protein of silk.
- The figure below shows both types of secondary structures
in a single protein.
Tertiary Structure
- refers to the bending and folding of the protein into a
specific three-dimensional shape.
- These structures result from four types of interactions
between the R side chains of the amino acids residues:
1. Disulfide bridges can form between two cysteine
residues that are close to each other in the same chain,
or between cysteine residues in different chains. These
bridges hold the protein chain in a loop or some other
3D shape.
2. Salt bridges are attractions between ions that result from
the interactions of the ionized side chains of acidic
amino acids (—COO-) and the side chains of basic
amino acids (—NH3 +).
3. Hydrogen bonds can form between a variety of side
chains, especially those that contain: Hydrogen bonding
also influences the secondary structure, but here the
hydrogen bonding is between R groups, while in
secondary structures it is between the C=O and NH
portions of the backbone.
4. Hydrophobic interactions result from the attraction of
nonpolar groups, or when they are forced together by
their mutual repulsion of the aqueous solvent. These
interactions are particularly important between the
benzene rings in phenylalanine or tryptophan. This type
of interaction is relatively weak, but since it acts over
large surface areas, the net effect is a strong interaction.
- The compact structure of globular proteins in aqueous
solution, in which the nonpolar groups are pointed inward,
away from the water molecules.
Quaternary Structure
- When two or more polypeptide chains are held together by
disulfide bridges, salt bridges, hydrogen bond, or
hydrophobic interactions, forming a larger protein complex.
- Each of the polypeptide subunits has its own primary,
secondary, and tertiary structure.
- The arrangement of the subunits to form a larger protein is
the quaternary structure of the protein.
Hemoglobin
- made of four subunits: two identical alpha chains containing
141 AA’s and two identical beta chains containing 146 AA’s.
- Each subunit contains a heme group located in crevices near
the exterior of the molecule.
- A hemoglobin molecule in a person suffering from
sicklecell anemia has a one-amino acid difference in the
sixth position of the two b-chains of normal HbA (a
glutamate is replaced with a valine).
- This changes the shape of red blood cells that carry this
mutation to a characteristic sickle shape, which causes the
cells to clump together and wedge in capillaries, particularly
in the spleen, and cause excruciating pain.
- Cells blocking capillaries are rapidly destroyed, and the loss
of these red blood cells causes anemia.
Protein Hydrolysis
- Amides can be hydrolyzed under acidic or basic conditions.
- The peptide bonds in proteins can be broken down under
acidic or basic conditions into smaller peptides, or all the
way to amino acids, depending on the hydrolysis time,
temperature, and pH
- The digestion of proteins involves hydrolysis reactions
catalyzed by digestive enzymes.
- Cellular proteins are constantly being broken down as the
body resynthesizes molecules and tissues that it needs.
Protein Denaturation
- Proteins are maintained in their native state (their natural 3D
conformation) by stable secondary and tertiary structures,
and by aggregation of subunits into quaternary structures.
- Denaturation is caused when the folded native structures
break down because of extreme temps. or pH values, which
disrupt the stabilizing structures. The structure becomes
random and disorganized.
- Most proteins are biologically active only over a
temperature range of 00C to 400C.
- Heat is often used to kill microorganisms and deactivate
their toxins. The protein toxin from Clostridium botulinum
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 BIOCHEM – LECTURE
is inactivated by being heated to 1000C for a few minutes;
heating also deactivates the toxins that cause diphtheria and
tetanus.
- Heat denaturation is used to prepare vaccines against some
diseases. The denatured toxin can no longer cause the
disease, but it can stimulate the body to produce substances
that induce immunity.
- Proteins can also be denatured by heavy-metal ions such as
Hg2+, Ag+, and Pb2+ that interact with —SH and
carboxylate groups.
- Organic materials containing Hg (mercurochrome and
merthiolate) were common topical antiseptics.
- Heavy-metal poisoning is often treated with large
doses of raw egg white and milk; the proteins in the
egg and milk bind to the metal ions, forming a
precipitate, which is either vomited out or pumped out.

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 BIOCHEM – LECTURE
Characteristics of Protein Non-Polar Amino Acids
• A protein is a naturally-occurring, unbranched polymer in
which the monomer units are amino acids
• Proteins are most abundant molecules in the cells after
water – account for about 15% of a cell’s overall mass
• Elemental composition - Contain Carbon (C), Hydrogen
(H), Nitrogen (N), Oxygen (O), most also contain Sulfur
(S)
• The average nitrogen content of proteins is 15.4% by mass
• Also present are Iron (Fe), phosphorus (P) and some other
metals in some specialized proteins

Amino Acids: The building Blocks

- Amino acid - An organic compound that contains both an
amino (-NH2) and carboxyl (-COOH) groups attached to
same carbon atom Polar Neutral Amino Acids
• The position of carbon atom is Alpha (a)
• -NH2 group is attached at alpha (a) carbon atom.
• -COOH group is attached at alpha (a) carbon atom.
- R = side chain –vary in size, shape, charge, acidity,
functional groups present, hydrogen-bonding ability, and
chemical reactivity.
• >700 amino acids are known
• Based on common “R” groups, there are 20 standard
amino acids
- All amino acids differ from one another by their R-groups
- Standard amino acids are divided into four groups based on
the properties of R-groups
- Non-polar amino acids: R-groups are non-polar
• Such amino acids are hydrophobic-water fearing
(insoluble in water)
• 8 of the 20 standard amino acids are non polar
• When present in proteins, they are located in the Polar Acidic and Basic Amino Acids
interior of protein where there is no polarity
Polar amino acids: R-groups are polar
a) Polar-neutral: contains polar but neutral side chains
• Seven amino acids belong to this category
b) Polar acidic: Contain carboxyl group as part of the side
chains
• Two amino acids belong to this category
c) Polar basic: Contain amino group as part of the side chain
• Two amino acids belong to this category
Nomenclature
- Common names assigned to the amino acids are currently
used.
- Three letter abbreviations - widely used for naming:
• First letter of amino acid name is compulsory and
capitalized followed by next two letters not
capitalized except in the case of Asparagine (Asn),
Glutamine (Gln) and tryptophan (Trp).
- One-letter symbols - commonly used for comparing amino
acid sequences of proteins:
• Usually the first letter of the name
• When more than one amino acid has the same letter
the most abundant amino acid gets the 1st letter.

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 BIOCHEM – LECTURE
Chirality and Amino Acids Cysteine: A Chemically Unique Amino Acid
- Four different groups are attached to the a-carbon atom in Cysteine: the only standard amino acid with a sulfhydryl group
all of the standard amino acids except glycine (— SH group).
• In glycine R-group is hydrogen - The sulfhydryl group imparts cysteine a chemical property
- Therefore 19 of the 20 standard amino acids contain a chiral unique among the standard amino acids.
center - Cysteine in the presence of mild oxidizing agents dimerizes
- Chiral centers exhibit enantiomerism (left- and right-handed to form a cystine molecule.
forms) • Cystine - two cysteine residues linked via a covalent
- Each of the 19 amino acids exist in left and right-handed disulfide bond.
forms Peptides
- Under proper conditions, amino acids can bond together to
produce an unbranched chain of amino acids.
- The length of the amino acid chain can vary from a few
amino acids to many amino acids.
- The amino acids found in nature as well as in proteins are L - Such a chain of covalently-linked amino acids is called a
isomers. peptide.
• Bacteria do have some D-amino acids - The covalent bonds between amino acids in a peptide are
• With monosaccharides nature favors D-isomers called peptide bonds.
- The rules for drawing Fischer projection formulas for amino
acid structures
- The — COOH group is put at the top, the R group at the
bottom to position the carbon chain vertically
- The — NH2 group is in a horizontal position.
• Positioning — NH2 on the left - L isomer - Dipeptide: bond between two amino acids
• Positioning — NH2 on the right - D isomer. - Oligopeptide: bond between ~ 10 - 20 amino acids
- Polypeptide: bond between large number of amino acids
- Every peptide has an N-terminal end and a C-terminal end
+
H3N-aa-aa-aa-aa-aa-aa-aa-aa-aa-COO-
OH
N-terminal end
O O CH2 O
H H
+ C C CH C O-
H3N CH N CH N

CH3 CH2 C-terminal end

Acid-base Properties of Amino acids

- In pure form amino acids are white crystalline solids
- Most amino acids decompose before they melt
- Not very soluble in water
- Exists as Zwitterion: An ion with + (positive) and – Alanine Phenylalanine Serine
(Nagetive) charges on the same molecule with a net zero
Peptide Nomenclature
charge
- The C-terminal amino acid residue keeps its full amino acid
• Carboxyl groups give-up a proton to get negative
name.
charge
- All of the other amino acid residues have names that end in
• Amino groups accept a proton to become positive -yl. The -yl suffi x replaces the -ine or -ic acid ending of the
- Amino acids in solution exist in three different species amino acid name, except for tryptophan, for which -yl is
(zwitterions, positive ion, and negative ion) - Equilibrium added to the name.
shifts with change in pH - The amino acid naming sequence begins at the N-terminal
- Isoelectric point (pI) – pH at which the concentration of amino acid residue.
Zwitterion is maximum -- net charge is zero - Example:
• Different amino acids have different isoelectric points • Ala-leu-gly has the IUPAC name of
• At isoelectric point - amino acids are not attracted alanylleucylglycine
towards an applied electric field because they net zero Isomeric Peptides
charge. - Peptides that contain the same amino acids but present in
COOH COO- COO-
different order are different molecules (constitutional
+H N +
3 H H3N H H2N H isomers) with different properties
• For example, two different dipeptides can be formed
CH3 CH3 CH3
between alanine and glycine
Low pH Zwitter Ion High pH
(net + charge) (net neutral charge)
(net - charge) - The number of isomeric peptides possible increases rapidly
as the length of the peptide chain increases
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 BIOCHEM – LECTURE
Protein Classification Based on Chemical Composition
- Simple proteins: A protein in which only amino acid
residues are present:
• More than one protein subunit may be present but all
subunits contain only amino acids
- Conjugated protein: A protein that has one or more non-
Biochemically Important Small Peptides amino acid entities (prosthetic groups) present in its
Many relatively small peptides are biochemically active: structure:
Hormones • One or more polypeptide chains may be present
Neurotransmitters
• Non-amino acid components - may be organic or
Antioxidants
inorganic - prosthetic groups
Small Peptide Hormones:
• Lipoproteins contain lipid prosthetic groups
Best-known peptide hormones: oxytocin and
• Glycoproteins contain carbohydrate groups,
vasopressin
Produced by the pituitary gland • Metalloproteins contain a specific metal as prosthetic
nonapeptide (nine amino acid residues) with six of the group
residues held in the form of a loop by a disulfide bond Four Types of Structures
formed between two cysteine residues Primary Structure
Small Peptide Neurotransmitters - refers to the order in which amino acids are linked together
- Enkephalins are pentapeptide neurotransmitters produced in a protein
by the brain and bind receptor within the brain - Every protein has its own unique amino acid sequence
- Help reduce pain • Frederick Sanger (1953) sequenced and determined
- Best-known enkephalins: the primary structure for the first protein - Insulin
• Met-enkephalin: Tyr–Gly–Gly–Phe–Met Primary Structure of a Human Myoglobin:
• Leu-enkephalin: Tyr–Gly–Gly–Phe–Leu
Small Peptide Antioxidants
- Glutathione (Glu–Cys–Gly) – a tripeptide – is present is in
high levels in most cells
- Regulator of oxidation–reduction reactions.
- Glutathione is an antioxidant and protects cellular contents
from oxidizing agents such as peroxides and superoxides
• Highly reactive forms of oxygen often generated
within the cell in response to bacterial invasion
- Unusual structural feature – Glu is bonded to Cys through
the side-chain carboxyl group.

- Proteins of the same organism always same sequence (cows,

pigs, etc.)
- Different sources: Insulin from pigs, cows, sheep, humans
General Structural Characteristics of Proteins similar
- General definition: A protein is a naturally-occurring, - Some differences:
unbranched polymer in which the monomer units are amino Species Chain A Chain B
acids.
- Specific definition: A protein is a peptide in which at least
AA #8 AA #9 AA AA #30
40 amino acid residues are present: #10
• The terms polypeptide and protein are often used Human Thr Ser Ile Thr
interchangeably used to describe a protein Pig Thr Ser Ile Ala
• Several proteins with >10,000 amino acid residues (porcine)
• are known Cow Ala Ser Val Ala
Common proteins contain 400–500 amino acid residues
• Small proteins contain 40–100 amino acid residues (bovine)
- More than one peptide chain may be present in a protein:
• Monomeric: A monomeric protein contains one - Due to differences insulin may show some reaction over
peptide chain time
• Multimeric: A multimeric protein contains more than - Now human insulin produced from genetically engineered
one peptide chain bacteria

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 BIOCHEM – LECTURE
Secondary Structure of Proteins
- Arrangement of atoms of backbone in space.
- The two most common types: alpha-helix (a-helix) and the
beta-pleated sheet (b-pleated sheet).
- The peptide linkages are essentially planar thus allows only
two possible arrangements for the peptide backbone for the
following reasons:
• For two amino acids linked through a peptide bond
six atoms lie in the same plane
• The planar peptide linkage structure has considerable
rigidity, therefore rotation of groups about the C–N
bond is hindered
• Cis–trans isomerism is possible about C–N bond.
• The trans isomer is the preferred orientation
Alpha-helix (a-helix)
- A single protein chain adopts a shape that resembles a
coiled spring (helix):
• H-bonding between same amino acid chains –intra
molecular
• Coiled helical spring
• R-group outside of the helix -- not enough room for
them to stay inside
Beta-Pleated Sheets
- Completely extended amino acid chains
- H-bonding between two different chains – inter and/or
intramolecular
- Side chains below or above the axis
Tertiary Structure of Proteins
- The overall three-dimensional shape of a protein
- Results from the interactions between amino acid side
chains (R groups) that are widely separated from each other.
- In general, 4 types of interactions are observed.
1) Disulfide bond: covalent, strong, between two cysteine
groups
2) Electrostatic interactions: Salt Bridge between charged
side chains of acidic and basic amino acids
• -OH, -NH2, -COOH, -CONH2
3) H-Bonding between polar, acidic and/or basic R groups
• For H-bonding to occur, the H must be
attached on O, N or F
4) Hydrophobic interactions: Between non-polar side
chains
Quaternary Structure of Proteins
- refers to the organization among the various peptide chains
in a multimeric protein:
• Highest level of protein organization
• Present only in proteins that have 2 or more
polypeptide chains (subunits)
• Subunits are generally Independent of each other -
not covalently bonded
• Proteins with quartenary structure are often referred
to as oligomeric proteins
• Contain even number of subunits
Protein Classification Based on Shape
- Three types of proteins: fibrous, globular, and membrane
- Fibrous proteins: protein molecules with elongated shape:
• Generally insoluble in water
• Single type of secondary structure
• Tend to have simple, regular, linear structures
• Tend to aggregate together to form macromolecular
structures, e.g., hair, nails, etc
- Globular proteins: protein molecules with peptide chains
folded into spherical or globular shapes:
• Generally, water soluble – hydrophobic amino acid
residues in the protein core
• Function as enzymes and intracellular signaling
molecules
- Membrane proteins: associated with cell membranes
• Insoluble in water – hydrophobic amino acid residues
on the surface
• Help in transport of molecules across the membrane
Fibrous Proteins: Alpha-Keratin
- Provide protective coating for organs
- Major protein constituent of hair, feather, nails, horns and
turtle shells
- Mainly made of hydrophobic amino acid residues
- Hardness of keratin depends upon -S-S- bonds
- more –S-S– bonds make nail and bones hard
Fibrous Proteins: Collagen
- Most abundant proteins in humans (30% of total body
protein)
- Major structural material in tendons, ligaments, blood
vessels, and skin
- Organic component of bones and teeth
- Predominant structure - triple helix
- Rich in proline (up to 20%) – important to maintain structure
Globular Proteins: Myoglobin
An oxygen storage molecule in muscles.
Monomer - single peptide chain with one heme unit
Binds one O2 molecule
Has a higher affinity for oxygen than hemoglobin.
Oxygen stored in myoglobin molecules serves as a reserve
oxygen source for working muscles
Globular Proteins: Hemoglobin
- An oxygen carrier molecule in blood
- Transports oxygen from lungs to tissues
- Tetramer (four peptide chains) - each subunit has a heme
group
- Can transport up to 4 oxygen molecules at time
- Iron atom in heme interacts with oxygen
Protein Classification Based on function
- Proteins play crucial roles in most biochemical processes.
- The diversity of functions exhibited by proteins far exceeds
the role of other biochemical molecules
- The functional versatility of proteins stems from:
• Ability to bind small molecules specifically and strongly
• Ability to bind other proteins and form fiber-like
structures, and
• Ability integrated into cell membranes
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 BIOCHEM – LECTURE
Major Categories of Proteins Based on Function
- Catalytic proteins: Enzymes are best known for their
catalytic role.
• Almost every chemical reaction in the body is driven
by an enzyme
- Defense proteins: Immunoglobulins or antibodies are
central to functioning of the body’s immune system.
- Transport proteins: Bind small biomolecules, e.g., oxygen
and other ligands, and transport them to other locations in
the body and release them on demand.
- Messenger proteins: transmit signals to coordinate
biochemical processes between different cells, tissues, and
organs.
• Insulin and glucagon - regulate carbohydrate
metabolism
• Human growth hormone – regulate body growth
- Contractile proteins: Necessary for all forms of movement.
• Muscles contain filament-like contractile proteins
(actin and myosin).
• Human reproduction depends on the movement of
sperm – possible because of contractile proteins.
- Structural proteins: Confer stiffness and rigidity
• Collagen is a component of cartilage a
• Keratin gives mechanical strength as well as
protective covering to hair, fingernails, feathers,
hooves, etc.
- Transmembrane proteins: Span a cell membrane and help
control the movement of small molecules and ions.
• Have channels – help molecules can enter and exist
the cell.
• Transport is very selective - allow passage of one
type of molecule or ion.
- Storage proteins: Bind (and store) small molecules.
• Ferritin - an iron-storage protein - saves iron for use
in the biosynthesis of new hemoglobin molecules.
• Myoglobin - an oxygen-storage protein present in
muscle
- Regulatory proteins: Often found “embedded” in the
exterior surface of cell membranes - act as sites for receptor
molecules
• Often the molecules that bind to enzymes (catalytic
proteins), thereby turning them “on” and “off,” and
thus controlling enzymatic action.
- Nutrient proteins: Particularly important in the early stages
of life - from embryo to infant.
• Casein (milk) and oval albumin (egg white) are
nutrient proteins
• Milk also provides immunological protection for
mammalian young.
Protein Hydrolysis
Hydrolysis of proteins - reverse of peptide bond formation:
Results in the generation of an amine and a carboxylic
acid functional groups.
Digestion of ingested protein is enzyme-catalyzed
hydrolysis
Free amino acids produced are absorbed into the
bloodstream and transported to the liver for the synthesis
of new proteins.
Hydrolysis of cellular proteins and their resynthesis is a
continuous process.
Protein Denaturation
- Partial or complete disorganization of protein’s tertiary
structure
- Cooking food denatures the protein but does not change
protein nutritional value
- Coagulation: Precipitation (denaturation of proteins)
• Egg white - a concentrated solution of protein
albumin - forms a jelly when heated because the
albumin is denatured
- Cooking:
• Denatures proteins – Makes it easy for enzymes in
our body to hydrolyze/digest protein
• Kills microorganisms by denaturation of proteins
• Fever: >104ºF – the critical enzymes of the body
start getting denatured
Glycoproteins
- Conjugated proteins with carbohydrates linked to them:
• Many of plasma membrane proteins are
glycoproteins
• Blood group markers of the ABO system are also
glycoproteins
• Collagen and mmunoglobulins are glycoproteins
- Collagen - glycoprotein
• Most abundant protein in human body (30% of total
body protein)
• Triple helix structure
• Rich in 4-hydroxyproline (5%) and 5-hydroxylysine
(1%) — derivatives
• Some hydroxylysines are linked to glucose, galactose,
and their disaccharides – help in aggregation of
collagen fibrils.
Immunoglobulins
- Glycoproteins produced as a protective response to the
invasion of microorganisms or foreign molecules -
antibodies against antigens.
- Immunoglobulin bonding to an antigen via variable region
of an immunoglobulin occurs through hydrophobic
interactions, dipole – dipole interactions, and hydrogen
bonds.
Lipoprotein
- a conjugated protein that contains lipids in addition to amino
acids
- Major function - help suspend lipids and transport them
through the bloodstream
- Four major classes of plasma lipoproteins:
• Chylomicrons: Transport dietary triacylglycerols
from intestine to liver and to adipose tissue.
• Very-low-density lipoproteins (VLDL): Transport
triacylglycerols synthesized in the liver to adipose
tissue.
• Low-density lipoproteins (LDL): Transport
cholesterol synthesized in the liver to cells throughout
the body.
• High-density lipoproteins (HDL): Collect excess
cholesterol from body tissues and transport it back to
the liver for degradation to bile acids.
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