Organic Macromolecules

Carbohydrates, Lipids, Proteins,

Enzymes, Nucleic Acids, ATP and
Micronutrients
 Organic Macromolecules

 Organic compounds are comprised of C, H and usu. O

 Organic chemicals found in living organisms come in
four categories:
 Carbohydrates – sugars in humans/ starches in plants
 Lipids – fats, phospholipids and steroids
 Proteins – amino acids
 Nucleic Acids – RNA and DNA
 These molecules are called macromolecules.
 They are composed of subunits called monomers, which
join together to form polymers.
 I. Carbohydrates

Carbohydrates (sugars)
 Major source of energy for cellular
metabolism; body uses carbohydrates first for
fuel
 Chemical formula: C1H2O1
 The energy is stored in the bonds between the
6 carbon, 12 hydrogen, and 6 oxygen atoms
in the glucose sugar molecule.
 Glucose is a monosaccharide, consisting of a
single ring structure.
 Carbohydrates

Most common form in the body

FIGURE 2–10 The Structure of Glucose.

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 Simple Carbohydrates
 Monosaccharides-simple sugars with 3 to 7 carbon
atoms
 Glucose (Glu)-6 carbon hexose
 Galactose (Gal)
 Fructose (Fru)-found in fruit and male reproductive tract;
5 carbon pentose
 Simple Carbohydrates
 Disaccharides
 Two simple sugars condensed by dehydration
synthesis
 Sucrose=glu+fru
 Maltose=glu+glu
 Lactose=glu+gal
 Carbohydrates

sucrase

FIGURE 2–11 The Breakdown of Complex Sugars.

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 Carbohydrates

FIGURE 2–11 The Breakdown of Complex Sugars.

Copyright © 2009 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

 Complex Carbohydrates
 Polysaccharides
 Many monosaccharides condensed by dehydration
synthesis to form a polymer
 Form polysaccharides by dehydration synthesis in
body
 Take more time to digest
 Glycogen-storage form of glc in animals that is
stored in liver and skeletal muscle
 Starch-storage form of glc in plants that is stored in
roots (most we can digest)
 Cellulose-component of plant cell wall that we
cannot digest
 Complex Carbohydrates
 Dehydration synthesis reactions occur
between glucose molecules to form
glycogen branches
 Glycogen

FIGURE 2–12 The Structure of the Polysaccharide Glycogen.

Copyright © 2009 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

 Complex Carbohydrates
 Cellulose-insoluble dietary fiber that keeps
your digestive tract moving.
 Soluble dietary fiber (oat bran, legumes, fruits
and veggies) slows down digestion, protects
blood vessels, decreases cholesterol and the
risk of some cancers.
 What is soluble fiber?
Simple vs. Complex Carbs
 II. Lipids
 Made mostly of carbon and hydrogen atoms
 Partially or entirely hydrophobic molecules
 Some do have polar groups on one end and
non-polar groups on the other end (amphipathic)
 Use lipids as fuel after exhaust carb source
 Provide twice the energy carbs do-so need less
http://www.medicine-raw-materials.com/others/page_8.html

http://www.chem.ucalgary.ca/courses/350/Carey5th/Ch26/ch26-1-2.html
 Lipids

 Lipids need transport proteins to go into blood

because they are not water soluble
 Most lipids are transported by some type of
lipoproteins (LDL and HDL)
 Free fatty acids are transported by albumin (made by
liver)
 Examples of lipids: triglycerides, phospholipids,
eicosanoids, and steroids.
 IIA. Triglycerides
 Triglycerides= glycerol backbone + 3 fatty acid tails
 Non polar, so they have transport proteins called very low
density lipoproteins (VLDL) to transport them in blood
 What we typically call “fats”
– We eat them, they are stored in adipocytes as energy reserves;
fatty acid tails are broken down for fuel

 Have four important functions:

– Used as fuel
– Protect internal organs
– Use as insulation so you lose less heat to environment
– Attract and store lipid-soluble vitamins A, D, E & K, drugs, and
toxins (Hg & DDT)**
Triglyceride Structure
Triglyceride Formation
 Fatty Acids

 Fatty Acids/ Fatty Acid Tails

 Long chains of carbon and hydrogen with a
carboxylic acid group (COOH) at one end
 Hydrocarbon chain is nonpolar while the
carboxylic acid group is polar
 Fatty Acids
Hydrocarbon tail

Carboxyl
group
 Fatty Acids
 Fatty Acids
 Breaking the C-C bond yields energy; since
there are more bond than in carbs you get more
energy
 Most we can synthesize but some we must get
from our diet
 Characterized by chain length (short, medium or
long-chain fatty acids) & number of double bonds
(saturated, unsaturated, or polyunsaturated fatty
acids)
 Essential Fatty Acids
 Fatty Acids
 Omega-3 and omega-6 are essential fatty acids.
They must be obtained from the diet.
 Omega-3 fatty acids are associated with
healthy brain and nerve function and decreased
body inflammation.
 Eicosapentaenoic, docasahexaenoic, and alpha
linolenic acids
 Found in salmon, sardines, flax seed, and walnuts
 Essential Fatty Acids
 Omega-6 fatty acids are associated with
inflammation. We can produce small amounts
of this f.a.
 Omega-6 f.a. are found in eggs, animal meat, and
vegetable oil.
 We get enough omega-6 from our diet; we
need more omega-3 in our diet.
Saturated vs. Unsaturated Fatty Acids
 Fatty acids/fatty acid tails can be:
 Saturated (no double bonds between carbons)
 All carbons have the max amount of H’s
bonded
 Unsaturated (one or more double bonds in the
fatty acid chain):
 monounsaturated = one double bond
 polyunsaturated = two or more double bonds
Saturated vs. Unsaturated Fatty Acids
Saturated vs. Unsaturated Fatty Acids
 The single bonds in saturated
fats/saturated fatty acid tails allow the fats
to pack together tightly. That is why they
are solid at room temperature.

 The double bonds in unsaturated fats make

the fatty acid tails kink. Thus, they are
liquid at room temperature.
 Vegetable oils are unsaturated fats.
 Plants tend to be richer in unsaturated fats
than animals.
Saturated vs. Unsaturated Fatty Acids

 Excess saturated fat intake is associated

with several diseases
 Nutritionists recommend that the amount
of fat in our diet be limited to 30%
 Fewer negative health effects are
associated with unsaturated fats
 Unsaturated fats require more energy to
break down
 Unsaturated fat= liquid at
room temperature

Saturated fat= solid at room

temperature
 Cis and Trans Unsaturated Fats
 cis configuration – when the hydrogen atoms
are on the same side of the carbon to carbon
double bond. These occur in nature.
 trans configuration – when the hydrogen
atoms are on opposite sides of the double
bond.
 These are not found in nature.
 These are the source of potential health risks.
 The conformation of the trans fat helps it adhere
to artery walls and form plaque.
 • Plaque formation
in arteries is due
to high levels of
trans fats,
triglycerides, and
cholesterol

• Is plaque
formation
reversible?

http://www.zimbio.com/Cell+Membranes+and+Adhesion/articles/8/Cholesterol
 IIB. Phospholipids

 Phospholipids
 Phospholipids= phosphate group + 2 fatty acid tails

 It is a diglyceride (has 2 fatty acid tails)

 It has a hydrophilic head and hydrophobic tail

 Main component of cellular membrane

 Phospholipids

FIGURE 2–17 Phospholipids and Glycolipids.

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 Phospholipids

FIGURE 2–17 Phospholipids and Glycolipids.

Copyright © 2009 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

Phospholipids
 IIC. Eicosanoids
 Eicosanoids
 Prostaglandins, leukotrienes, and thromboxanes
 Derived from arachidonic acid which is an omega-
6 fatty acid (essential fatty acid)
 They act as local messengers (autocrine and
paracrine) for inflammation and immunity
 Act on endothelium, platelets, uterine and mast
cells
 Example: injured cells release these to trigger
nerve endings so you feel pain
 Eicosanoids

FIGURE 2–14 Prostaglandins.

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 IID. Steroids
 Steroids
 Made up of four fused carbon-containing rings with
variable side groups
 Cholesterol:
 Precursor to other steroids
 component of plasma (cell) membranes; aids with stability
 obtain from diet or synthesize in body
 Estrogens and testosterone:
 sex hormones
 Corticosteroids and calcitriol (vitamin D):
 metabolic regulation and calcium absorption
 Bile salts:
 derived from steroids
Testosterone + Estrogen
 Cholesterol
 Cholesterol is insoluble in water. It is carried
throughout the body attached to proteins
called lipoproteins.
 Lipoproteins have three parts:
 Core composed of cholesterol esters and
triacylglycerols
 Surface monolayer composed of phospholipids
and cholesterol
 On top of surface layer is an apoprotein
 chm.bris.ac.uk

• Low-density lipoproteins (LDLs) are high in

cholesterol and low in protein. LDLs carry cholesterol
and triglycerides from liver to body cells.
• High density lipoproteins (HDLs) contain more protein
that cholesterol. They scavenge excess cholesterol from
the body and return it to the liver.
 Cholesterol

 The LDL/HDL ratio is an index of the rate at

which cholesterol leaves cells and returns to the
liver.
 A low ratio is good, indicating that less
cholesterol is in the bloodstream.

Copyright © 2009 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

 • Plaque formation
in arteries is due
to high levels of
trans fats,
triglycerides, and
cholesterol

• Is plaque
formation
reversible?

http://www.zimbio.com/Cell+Membranes+and+Adhesion/articles/8/Cholesterol
Normal blood plasma values for cholesterol
and triglycerides…

•Total cholesterol ratio

(LDL:HDL)
<200 mg/ 100 ml of plasma
•HDL >60 mg/ 100 ml of plasma
•LDL <100 mg/ 100 ml of plasma

•Triglycerides <150 mg/ 100 ml of

plasma
 III. Proteins

 Proteins are the most abundant and

important organic molecules
 Contain basic elements
 Carbon (C), hydrogen (H), oxygen (O), and
nitrogen (N)

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 Proteins
 Seven major protein functions

 Support  Buffering
 Structural proteins  Regulation of pH
 Movement  Metabolic regulation
 Enzymes
 Contractile proteins
 Coordination and
 Transport
control
 Transport (carrier)  Hormones
proteins
 Defense
 Antibodies

Copyright © 2009 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

 Proteins

 Composed of amino acids

 There are 20 different amino acids; most
can be synthesized by the body
 Those the body cannot synthesize are
called essential amino acids; these must
come from the diet
 Protein-rich foods include beef, poultry,
fish, beans, eggs, nuts, and dairy products
such as milk, yogurt, and cheese.
Amino Acids

Table 2.4
 Amino Acids

 Amino acid structure

 All amino acids have the same:
 Central carbon atom
 Hydrogen atom
 Amino group (—NH2)
 Carboxylic acid group (—COOH)

 The variable side chain or R group is different for

each amino acid
Amino Acid Structure
 Amino Acids

 Each particular amino acid has its own

variable side chain (R-group)
 The side group gives the amino acid its
chemical properties; they can be polar,
non-polar, positively charged, or negatively
charged
Amino Acids

Table 2.4
 Proteins

 Hooking amino acids together requires

 A dehydration synthesis between
 The amino group of one amino acid
 And the carboxylic acid group of another amino
acid
 This produces a peptide

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 Proteins

FIGURE 2–19 The Formation of Peptide Bonds.

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 Protein Folding Sequence

 Protein folding sequence:

 Primary structure
 The sequence of amino acids along a polypeptide
 Secondary structure
 Hydrogen bonds form-helix or -pleated sheet
 Tertiary structure
 Secondary structure folds into a unique shape
 Quaternary structure
 Final protein shape:
– several tertiary structures together
Copyright © 2009 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
 Primary Structure
 Primary structure-the linear sequence of
amino acids in a peptide chain
 Long polymers of amino acids are named
polypeptides because the covalent bond
joining the amino acids in the chain is a
peptide bond.
 Secondary Structure
 Secondary protein structure – the
polypeptide folds on itself in a regular
pleated fashion.
 Folding produce helical structures (-
helices) or accordion-like pleats (-pleated
sheets).
 Secondary structures result from hydrogen
bonding between the amino group of one
amino acid and the carboxyl group of
another.
 Secondary Structure

FIGURE 2–20 Protein Structure.

Copyright © 2009 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

 Tertiary Structure
 Tertiary structure-comes from the
interaction of the amino acid side groups
 These interactions involve hydrogen, ionic
and covalent bonds
 Side groups interact with one another to affect
the three-dimensional structure of the protein
Hemoglobin
 Quaternary Structure
 Quaternary structure-two or more tertiary
structures bound together
 Gives protein it’s final shape
 Structure determines function
Hemoglobin
 Proteins

 Two structural classes of proteins:

 Fibrous proteins (keratin)-structural sheets or
strands (STRONG!)
 Globular proteins (hemoglobin)

 Soluble spheres with active functions

 Protein function is based on shape

 Shape is based on sequence of amino acids

 Proteins

FIGURE 2–20 Protein Structure.

 Protein Function

 Proteins serve many important functions:

 Proteins called enzymes speed up chemical
reactions. Enzymes are also components of
cell membranes.
 Proteins regulate gene expression in cells
 Proteins are important structural components
of cells
 Proteins (hormones) function as chemical
messengers.
How long would it take to digest this?
 Enzymes

 Enzymes – proteins that speed up

(catalyze) the rate of chemical reactions,
thus liberating the energy stored in the
bonds of food.
 The speed and efficiency of the enzyme
affects the rate a person can metabolize food.
 Enzymes lower the ENERGY requirements for
chemical reactions to occur, so that the
reactions can occur more quickly.
 Enzymes Are Used In:

 Decomposition reaction (catabolism)

 Breaks chemical bonds
 AB A + B
 Hydrolysis: ABCDE + H2O ABC—H + HO—DE
 Synthesis reaction (anabolism)
 Forms chemical bonds
 A + B AB
 Dehydration synthesis (condensation)
ABC—H + HO—DE ABCDE + H2O
 Enzymes

 How do enzymes work?

They decrease the activation energy of
the reaction

 Activation energy – the energy required

to start a chemical reaction.

 Enzymes catalyze metabolic reactions by

decreasing this activation energy barrier.
 Enzymes

FIGURE 2–7 The Effect of Enzymes on Activation Energy.

 Enzymes

 Substrates – chemicals metabolized by

enzyme-catalyzed reactions
 Enzymes decrease the activation energy
barrier by binding to their substrate and
stressing its bonds to decrease the energy
required to break the bonds.
 Active site – location on the enzyme
where the substrate binds.
How an enzyme works:

http://www.nd.edu/~aostafin/CRCD/DOSS/enzymeanimation2.gif
Induced fit – a shape change in the enzyme
in response to substrate binding

Figure 3.25
 Enzymes

 Enzymes show specificity in the reactions

they can catalyze.
 Specificity is the result of the unique shape
of different enzymes because of their
amino acid sequences.
 Enzymes can be regulated
 Enzymes
 Sometimes enzymes need cofactors or
coenzymes to become active:
 Cofactors are ions of metal elements or
organic molecules (Mg+2, ATP)
 Coenzymes are cofactors that are derived
from vitamins (ATP, coenzyme A, FAD and
NAD-in metabolism)
 Enzymes
 Enzymes only work as fast as they can…
 You can saturate an enzyme
 v= velocity of reactants products
 Vmax=maximum velocity of enzyme
 [S]=substrate(s)/ reactant(s)
concentration(s)/level(s)
 Enzymes
 Enzymes can be
inhibited by:
 Heat-causes
denaturation
 Altering the surrounding
pH-each enzyme has a
specific pH it prefers
 Enzymes
 Enzymes can be inhibited by:
 Binding another molecule (inhibitor) in the active
site OR allosterically to another site that effects the
binding site
 Metabolic molecule like ATP
 Heavy metal (Hg)
 Drug
 IV. Nucleotides
 Nucleotides large organic molecules that form the genetic
material of the cell and are used in energy transfer for the
cell
 Nucleotides comprise:
 Deoxyribonucleic acid (DNA)
 Ribonucleic acid (RNA)
 Adenosine monophosphate (AMP)
 Examples of related molecules:
 Adenosine triphosphate (ATP); cyclic adenosine monophosphate
(cAMP)
 Nicotinamide adenine dinucleotide (NAD) and flavin adenine
dinucleotide (FAD)
 General Nucleotide Structure

FIGURE 2–22 Nucleotides and Nitrogenous Bases.

 Nitrogenous Base Options

FIGURE 2–22 Nucleotides and Nitrogenous Bases.

Copyright © 2009 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

 Nitrogenous Base Options

FIGURE 2–22 Nucleotides and Nitrogenous Bases.

Copyright © 2009 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

 Sugar Options

*sugar used in DNA *sugar used in RNA

http://www.mun.ca/biology/scarr/Deoxyribose_versus_Ribose.html
 Nucleic Acids

 Deoxyribonucleic Acid (DNA)

 Comprised of two strands of complementary
chains of nucleotides
 Nucleotide=phosphate + deoxyribose sugar +
nitrogenous base
DNA Nucleotides

Figure 2.22c
 DNA

A=T

C=G

http://evolution.berkeley.edu/
evolibrary/article/history_22
 DNA

 Deoxyribonucleic Acid (DNA)

 Stores genetic information in the form of genes
 DNA genes  chromosomes
 Function:
 Duplicate DNA for cell division OR
 Use as a “template” for protein synthesis
 Carries inherited characteristics, and controls enzyme
production and metabolism
 RNA
 Ribonucleic Acid (RNA)
 RNA takes the codes from DNA and translates it
into proteins.
 RNA is single stranded, has a ribose sugar, and
contains uracil (U) instead of thymine.
 mRNA takes the codes from DNA and translates
it into proteins.
 Messenger RNA
 transfer RNA
 ribosomal RNA
 Nucleosides
 Nucleosides can be used to store energy (ATP), to
transfer energy (FAD/ NAD), or as a messenger
(cAMP):
 Adenosine monophosphate (AMP) has one phosphate
group attached
 Adenosine diphosphate (ADP) has two phosphate groups;
di= 2
 Adenosine triphosphate (ATP) has three phosphate groups
 Nucleosides
 Nucleosides can be used to store energy (ATP), to
transfer energy (FAD/ NAD), or as a messenger
(cAMP):
 An ATPase is an enzyme that catalyzes phosphorylation
(the addition of a high-energy phosphate group to a
molecule) or needs ATP to do work
 FAD and NAD are electron carriers in metabolism
 Cyclic AMP is used in the cell as a secondary messenger
system for outside communication inside the cell
NAD+= electron carrier in metabolism
 Micronutrients

 Substances such as vitamins and minerals

are required in small amounts by the body.
 V. Micronutrients
 Vitamins
 13 essential vitamins
 Most can’t be synthesized by the body (D & K
are the exceptions)
 Function as coenzymes to help speed up
chemical reactions
 Vitamin deficiencies can affect every cell in the
body
 Micronutrients

 Vitamin D is synthesized in the body using

sunlight
 Vitamin D deficiency disrupts Ca+2 absorption in
intestine and bone growth
 You can get vitamin D in dairy products
http://www.scientificpsychic.com/health/vitamins.html
 Micronutrients
 Vitamin K is required for proper blood
clotting.
 It is not produced by human cells but comes
from bacteria living in our large intestine and
green-leafy vegetables
 The drug coumadin prevents blood clots by
inhibiting vitamin K synthesis
 If patients are on coumadin they should not
eat green-leafy vegetables, why?
 Micronutrients
 Hydrophilic vitamins can be dissolved in
plasma
 Therefore they are not stored in the body;
they are excreted in the urine
 Hydrophobic vitamins are not soluble in
water
 Hydrophobic vitamins (A, D, E and K) are
stored in our body fat
 It is possible to have an excess of these fat-
soluble vitamins in body tissues; this can
result in toxicity
Micronutrients

Table 2.6
 Micronutrients

 Minerals
 Do not contain carbon (inorganic), but are
essential for normal cell functions.
 Necessary for proper fluid balance, muscle
and nerve function, and building bones and
teeth
 Examples are calcium, chloride, sulfur,
magnesium, phosphorous, and potassium.
 Must be supplied through the diet
Micronutrients

Table 2.7
 Micronutrients

 Antioxidants
 Protect cells and tissues from damage caused
by highly reactive substances called free
radicals, which have an incomplete outer
electron shell and can thus oxidize (remove
electrons from) other molecules.
 Antioxidants bind free radicals and prevent
them from doing damage.
 Several vitamins and minerals are antioxidants.