PROTEINS

STANDARD AMINO ACID2

- Is one of the 20 a-amino acids
PROTEIN
normally found in proteins
- Naturally occurring unbranched
- Necessary constituents of human
polymer in which the monomer
proteins
units are amino acids
- Most abundant substance in nearly
all cells
4 CATEGORIES OF STANDARD AMINO
- 15% of a cell’s overall mass
ACIDS
CASEIN
1. NONPOLAR AMINO ACID
- Main protein of milk contains
- one amino group, one carboxyl
phosphorus, an element very
group and a nonpolar side chain
important in the diet of infants and
- Hydrophobic (not attracted to water
children
molecules)
- Found in meat, fish, eggs (complete
- Found in the interior of proteins kay
dietary protein)
limited it contact with water
HEMOGLOBIN
TRYPTOPHAN
- Oxygen-transporting protein of the
- Borderline member of nonpolar
blood
amino acid group (why? water can
- Contains iron
weakly interact through hydrogen
boding with the NH ring location on
tryptophan’s side chain ring
AMINO ACIDS
structure)
- Organic compound that contains
both an amino (-NH₂) and a
2. POLAR NEUTRAL AMINO ACID
carboxyl (-COOH) group
- one amino group, one carboxyl
group and a side chain that is polar
A – AMINO ACIDS
but neutral
- Alpha amino acids
- Side chain of pnaa is neither acidic
- Is an amino acid in which the amino
nor basic
group and the carboxyl group are
- More soluble in water than nonpolar
attached to the a-carbon atom
amino acid
- Amino acids that are always found in
proteins
3. POLAR ACIDIC AMINO ACID
- one amino group, two carboxyl
group, the second carboxyl group
There are more than 700 naturally
being part of the side chain
occurring amino acids known but only 20 of
- Side chain bears a negative charge
them, called standard amino acids, are
normally found in proteins

4. POLAR BASIC AMINO ACID
- two amino groups and one carboxyl
group, the second group being part
of the side chain
- Side chain bears a positive charge
ESSENTIAL AMINO ACIDS
- Standard amino needed for protein
synthesis
- Obtained from dietary sources
because body cannot synthesize in
adequate amounts from other
substances
9 essential amino acids for adults and tenth
one is needed for growth in children
(kayano man 9 la ha adults? Because waray
ARGININE. Waray arginine para ha adults
kay diri hya essential amino acid for adults)
COMPLETE DIETARY PROTEIN
- Contains all the essential amino
acids relative to the body’s needs
- May or may not contain all the
nonessential amino acids
- Protein in animal sources are
complete dietary protein
- Gelatin = only 1 incomplete na
dietary protein na waray ha animal
source
- Soy is the only common plant
protein that is a complete dietary
protein
INCOMPLETE DIETARY PROTEIN
- Does not contain adequate amounts
relative to the body’s needs of one
or more essential amino acids
- Plant sources are incomplete dietary
proteins
- Lysine (wheat, rice, oats, and corn)
- Methionine (beans and peas)
- Tryptophan (corn and beans)
LIMITING AMINO ACID
- An amino acid that is missing or
present in inadequate amounts, in
an incomplete dietary protein
COMPLEMENTARY DIETARY
PROTEINS
- Are two or more incomplete dietary
proteins combined forming a
complete dietary protein
(pag it duha na incomplete dietary protein
ig combine, nakakaform na hya hin
complete dp. Ex. It rice kay incomplter pati
it beans. Kumaon ka ngan hito na duha
complete dp nat hra na combination ngaran
incomplete dp hya)
CHIRALITY AND AMINO ACIDS
a-Carbon atom
side chain
amino group
carboxyl group
- Four different groups are attached
to the a-carbon atom in all of the
standard amino acids except glycine,
where the R group is a hydrogen
atom

ACID-BASE PROPERTIES OF AMINO
ACIDS
- In pure form, amino acids are
crystalline solids with relatively high
decomposition points
- Amino acids decompose first before
they melt
ZWITTERION
- German term meaning “double ion”
- Molecule that has a positive charge
on one atom and a negative charge
on another atom, but which has no
net charge
- Net charge on zwitterion = 0
- Strong intermolecular forces
between positive and negative
centers of zwitterion = cause of the
high melting points of amino acids
ISOLECTRIC POINTS
- Ph at which amino acid exists
primarily in its zwitterion form
CYSTEINE: A CHEMICALLY
UNIQUE AMINO ACID
Cysteine
- Only standard amino acid that has a
side chain na sulfhydryl group (-SH
group)
- Molecule that is made up of two like
subunits
PEPTIDE
- Unbranched chain of amino acids
DIPEPTIDE
- Compound containing two amino
acids
TRIPEPTIDE
- Three amino acids
OLIGOPEPTIDE
- 10 – 20 amino acid residues
POLYPEPTIDE
- Long unbranched chain of amino
acids
PEPTIDE BOND
- Covalent bond between the
carboxyl group of a one amino acid
and the amino group of another
amino acid
SMALL PEPTIDE HORMONES
OXYTOCIN AND VASOPRESSIN
- Two best-known peptide hormones
- Produced in the pituitary gland
- Both are nonapeptides (nine amino
acid residues)
OXYTOCIN
- Regulates urine contractions
(pagpanak) and lactation (produce
milk in the mammary glands)

DIMERIZES VASOPRESSIN
- Combines with a similar molecule to - Excretion of water by the kidneys
form a dimer - Antidiuretic hormone

DIMER
SMALL PEPTIDE CONJUGATED PROTEIN
- One or more non-amino-acid
NUEROTRANSMITTERS entities present in the structure in
addition to one or more peptide
ENKEPHALINS chains
- Pentapeptide neurotransmitters
produced by the brain that bind to PROSTHETIC GROUP
brain receptor sites to reduce pain - Non-amino acid group present in
conjugated proteins
BEST KNOWN ENKEPHALINS
- Met – enkephalin
- Leu – enkephalin

Met-enkephalin: Tyr-Gly-Gly-Phe-Met
Leu-enkephalin: Tyr-Gly-Gly-Phe-Leu

GLUTATHIONE
- Antioxidant
- Protects cellular contents from
oxidizing agents such as peroxides
and superoxides PRIMARY PROTEIN STRUCTURE
- Order in which amino acids are
linked together in a protein
GENERAL STRUCTURAL CHARACTERISTICS
OF PROTEINS
SECONDARY PROTEIN STRUCTURE
2 CLASSIFICATIONS OF PROTEIN - Arrangement in space adopted by
the backbone portion of a protein
MONOMERIC PROTEIN
- Only one peptide chain is present COMMON TYPES:
- Alpha helix (a helix)
MULTIMERIC PROTEIN - Beta pleated sheet (B pleated
- More than one peptide chain is sheet)
present
ALPHA HELIX STRUCTRE
CLASSIFICATION OF PROTEIN BASED - Resembles a coiled spring
ON CHEMICAL COMPOSITION - Hydrogen bond = intramolecular
BETA PLEATED SHEET
SIMPLE PROTEIN - Two extended protein chain
- Only amino acid residues are segments from the same or different
present molecule are held together by
hydrogen bonds
- Hydrogen bond= either inter or intra
UNSTRUCTURED PROTEIN SEGMENT
Neither a-helix or b pleated sheet
TERTIARY STRUCTURE OF PROTEINS
TERTIARY PROTEIN STRUCTURE
- Overall three-dimensional shape of a
protein
INTERACTIONS RESPONSIBLE FOR
TERTIARY STRUCTURE
1. Disulfide bonds – strongest tertiary
structure interactions
2. Electrostatic attractions – also
called salt bridges, interaction
between acidic side chain and a
basic side chain
3. Hydrogen bonds – occur between
amino acids with polar R groups
4. Hydrophobic attractions – result
when 2 nonpolar side chains are
close to each other
QUATERNARY PROTEIN STRUCTURE
- Organization among the various
peptide subunits in a multimeric
protein
- Highest level of protein organization
PROTEIN HYDROLYSIS
-
PROTEIN DENATURATION
- Partial or complete disorganization
of a protein’s characteristic three-
dimensional shape
- Disruption of the second, tertiary
and quaternary structural
interaction (only primary it diri api
ha denaturation)
DENATURATING AGENTS FOR PROTEIN
(definition of each ha book p.147)
1. Heat
2. Microwave radiation
3. Ultraviolet radiation
4. Violet whipping or shaking
5. Detergent
6. Organic solvents
7. Strong acids and bases
8. Salts of heavy metals
9. Reducing agents
FIBROUS PROTEIN
- Molecules that have elongated
shape
GLOBULAR PROTEIN
- Molecules have peptide chains that
are folded into spherical or globular
shapes
MEMBRANE PROTEIN
- Protein that is found associated with
a membrane system of a cell
D
A – KERATIN
- Ada ha hair
- Abundant in nature
- Gibes protective covering ha hair
COLLAGEN
- Abundant of all protein in humans
- 30% of total body protein
- Triple helix structure
- Component of cartilage
HEMOGLOBIN
- Oxygen-transfer from the lungs to
the tissue

MYOGLOBIN
- Oxygen-storage for molecules in
muscles
MYOSIN & ACTIN
- Proteins present in the muscle
tissues of meat
PROTEIN CLASSIFICATION BASED ON
FUNCTION
1. Catalytic proteins
2. Defense proteins
3. Transport proteins
4. Messenger proteins
5. Contractile proteins
6. Structural proteins
7. Transmembrane proteins
8. Storage proteins
9. Regulatory proteins
10. Nutrient proteins
11. Buffer proteins
12. Fluid – balance proteins
GLYCOPROTEIN
- Protein that contains carbohydrates
or carbohydrate derivatives
- Collagen and immunoglobulins
IMMUNOGLOBULINS
- Is a glycoprotein that serves as a
protective response to the invasion
of microorganisms or foreign
molecules
ANTIGEN
- Foreign substance such as a
bacterium or virus that invades the
human body
ANTIBODY
- Biochemical molecule that
counteracts a specific antigen
LIPOPROTEIN
- Conjugated protein that contains
lipids in addition to amino acids
- Major function: to help suspend
lipids and transport them through
the bloodstream
- Insoluble in blood bcos of nonpolar
nature
PLASMA LIPOPROTEIN
- Lipoprotein that is involved in the
transport system for lipids in the
bloodstream
FOUR MAJOR CLASSES:
1. Chylomicrons – transport dietary
triacylglycerol from intestine to liver
2. Very low density lipoprotein (VLDL)
– transport triacylglycerol
synthesized in liver to adipose tissue
3. Low density lipoprotein (LDL) –
transport cholesterol synthesized in
the liver to cells
4. High density lipoprotein (HDL) –
collect excess cholesterol from body
tissues and transport back to liver
for degradation to bile acid