AMINO ACIDS AND PROTEIN AMINO ACIDS

PROTEIN  Building blocks of proteins

 Amine group (NH2) is attached to the C atom
 Derived from a Greek word that means “of first
next to the carboxyl group
importance”
Cellular Function of Proteins
a. Group of Amino Acid
 Enzymes
 According to the polarity of their side chains
o Are biological catalyst
 Hydrophobic Amino Acids
o Speed up chemical reaction
o Prefer contact with one another over
o Amylase, pepsin, trypsin, lipase
contact with water
 Antibodies o Generally found buried in the interior
o Also called immunoglobulins
of proteins, where they can associate
o Are specific protein molecules produced by with one another and remain isolated
specialized cells of the immune system with water
(plasma cells) in response to foreign bodies o 9 Hydrophobic Amino Acid
(antigens)  Glycine (Gly)
 Transport Proteins  Alanine (Ala)
o Carry materials from one place to another in  Valine (Val)
the body  Leucine (Leu)
 Transferrin, hemoglobin, myoglobin  Isoleucine (Ile)
 Regulatory protein  Methionine (Met)
o Controls many aspects of cell function,  Phenylalanine (Phe)
including metabolism reproduction  Tryptophan (Trp)
 Protein hormones  Proline (Pro)
 Structural proteins  Hydrophilic Acids
o Provide mechanical support to large animals o Attracted to polar water molecules
and provide them with their outer coverings o Are often found on the surfaces of
 Keratin proteins
 Movement proteins o 3 classes
o Are necessary for all forms of movements  Polar, neutral amino acid
 Myosin and actin  Negatively charged amino acid
 Nutrient Proteins  Positively charge amino acid
o Serves as sources of amino acids for embryos
or infants
 Albumin (egg)
 Casein (milk)
A. Polar, Neutral Amino Acid The Peptide Bond

a. Have R groups that have a high affinity for

 Amide group that links amino acids
water but that are not ionic at pH 7
 Dipeptide – the molecule formed by condensing
i. Serine (Ser, S)
two amino acids
ii. Threonine (Thr, T)
 N – Terminal Amino Acid – with a free N+H3
iii. Tyrosine (Tyr, Y)
 C – Terminal Amino Acid – With a free -COO-
iv. Cysteine (Cys, C)
group
v. Asparagine (Asn, N)
 Nomenclature
vi. Glutamine (Gln, Q)
o Peptides are named as derivatives of the
B. Negatively Charge Amino Acid
C-terminal amino acid, which receives it
a. Have ionized carboxyl groups in their side
entire name
chains
o Fore all other amino acids, the ending -
b. At pH 7 these amino acids have a net charge
ine is change to -yl
of -1

c. They are acidic amino acids because PRIMARY STRUCTRUE OF PROTEINS

ionization of the carboxylic acid releases a
 Is the amino acid sequence of the protein chain
proton
 It results from the covalent bonding between the
i. Aspartic Acid (Asp, D)
amino acids in the chain (peptide bonds)
ii. Glutamic Acid (Glu, E)
 Are translations of information contained in
C. Positively Charge Amino Acids
genes
a. At pH 7, have a net positive charge because

of their side chains contain positive groups SECONDARY STRUCTURE OF PROTEINS

b. Are basic because the side chain reacts with  Where the peptide chains are folded regularly

water, picking up a proton and releasing a  Is the result of hydrogen bonding between the
amide hydrogen and carbonyl oxygens of the
hydroxide anion
peptide bonds
i. Lysine (Lys) o Helix
ii. Arginine (Arg) o Pleated Sheet

iii. Histidine (His) TERTIARY STRUCTURE OF PROTEINS

 Three-dimensional Structure
 Polypeptide chain with its regions of secondary
structure further folds on itself
 o Disulfide bridge

QUATERNARY STRUCTURE OF PROTEINS

b. Nonessential amino acids
 Hemoglobin  Are those amino acids that can be
 With four individual globular peptide unites synthesized by the body and need
 2 identical alpha-subunits not be included in the diet

 2 identical beta-subunits i. Alanine

ii. Arginine (1)
CLASSES OF PROTEINS
iii. Asparagine
a. Fibrous Proteins iv. Aspartate
 Are tough, insoluble, and composed of fibers v. Cysteine (2)
and sheets vi. Glutamate
 Collagen, keratin, elastin, myosin, fibrins vii. Glutamine
b. Globular Proteins viii. Glycine

 Are water-soluble and have chains folded into ix. Histidine (1)

compact shapes x. Proline

 Hemoglobin, myoglobin, insulin, xi. Serine

immunoglobulins xii. Tyrosine (2)

c. Simple Protein c. Complete Protein

 A protein composed of only of amino acid  Protein derived from an animals

residues  It provides all of the essential and

nonessential amino acids
 Ribonuclease (124 amino acids), albumins
d. Incomplete Protein
d. Conjugated Proteins
 Derived from vegetable sources
 A protein that incorporates one or more non-
 It lacks a sufficient amount of one
amino acid unites in its structure
or more essential amino aids
 Glycoprotein, lipoprotein, metalloproteins
e. Dietary Proteins PHYSICAL AND CHEMICAL PROPERTIES OF
 Nutritional Classes of amino acid PROTEINS
a. Essential amino acids
a. Generally Tasteless
 Are those that cannot be synthesized
b. Mostly are colorless. Few are colored and
by the body and are required in the
crystalline
diet
c. Insoluble in fat solvents and present varied
i. Isoleucine
degrees of solubility in water, salt solution,
ii. Leucine
dilute acids, and alkalis
iii. Lysine
d. Mostly are with high molecular weight
iv. Methionine
e. Most of them form non-diffusible colloid
v. Phenylalanine
solutions of emulsoid type
vi. Threonine
f. Amphoteric – property of certain compounds
vii. Tryptophan
that bare both positive and negative charges
viii. Valine
 g. Most of them are labile and readily modified o May form bonds with negatively charged side
in solution when subjected to alterations in pH, chain groups
UV, heat, and organic solvents o this interferes with the salt bridges formed
h. Very reactive and highly specific between amino acid R group, resulting in loss
of conformation
DENATURATION OF PROTEINS
 Mechanical Stress
 Occurs when the organized structures of a globular o Stirring, whipping, or shaking can disrupt the
protein become completely disorganized
weak interactions that maintain protein
 Temperature
conformation
o As the temperature increases, increases the
HEMOGLOBIN MOLECULE
rate of molecular movement within the
solution and the bonds within the proteins  Is a tetramer composed of four polypeptide
begin to vibrate more violently. 56* - 60* subunits:
o Lose their characteristics 3-dimensional o 2 alpha – subunits
conformation and become completely o 2 beta – subunits
disorganized  Heme group – ion portion
o Coagulation occurs as the protein molecules o Can bind four molecules of oxygen
then unfold and become entangled; they have
IMMUMOGLOBULINS
aggregated to become a solid
 pH  Antibodies
o when the pH of a protein solution is above the  Produced by plasma cells
pl, all the protein molecules will have a net  Highly specific
negative surface charge  Has a memory
o below the pl, they will have a net positive  Can recognize “self” from “nonself”
charge  Contain 4 peptide chains that are connected by
o in either case, these like-charged molecules disulfide bonds and arranged in a Y-shaped
repel one another, and this repulsion helps quaternary structure
keep these very large molecules in solution o IgA
o at the pI the protein molecules no longer have o IgD
a net surface charge, as a result they no longer o IgE
strongly repel one another and are at their o IgG
least solution o IgM
 Organic Solvent
o p
 Detergents
o Have both a hydrophobic region and a polar
or hydrophilic region
 Heavy Metals
o Mercury or lead