[TRANS] LECTURE 3: PROTEINS

PROTEINS 9. Gln - promotes healthy brain function

● Most abundant substances in nearly all cells ● necessary for the synthesis of RNA and DNA molecules
10. Gly - Component of skin and beneficial for wound healing
● Naturally occurring, unbranched polymer in which the monomer
units are amino acids ● acts as neurotransmitter
11. His - Important for synthesis of red and white blood cells
o All proteins contain the elements:
▪ Carbon ● Improve blood flow
12. Thr - nIt helps promote equilibrium in the central nervous system
▪ Hydrogen
● aids in balancing state of emotion
▪ Oxygen
13. Asp - Enhances stamina
▪ Nitrogen
14. Pro - plays role in intracellular signaling.
▪ Sulfur
15. Arg - plays role in blood vessel relaxation
o Human cell - contains 9000 different kinds of proteins
o Human body - contains 100,000 different proteins
● -amino acid - carboxyl group and hydrogen atom are attached ACID-BASE PROPERTIES OF AMINO ACIDS
to carbon atom ● In pure form, amino acids are white cyrstalline solids with
o All amino acids are alpha-amino acids except Proline relatively high decomposition points (most amino acids
(imino acid) decompose before they melt)

CLASSIFICATION OF AMINO ACIDS ZWITTERION

1. Nonpolar amino acid - contains one amino group, one carboxyl
group, and a nonpolar side chain. G,A,V,L,I,P,F,M,W
2. Polar neutral amino acid - contains one amino group, one carboxyl
group, and a side chain that is polar but neutral S,C,N,T,Q,Y
3. Polar basic amino acid - contains two amino groups and one
carboxyl group. H,K,R
4. Polar acidic amino acid - contains one amino group and two
carboxyl groups, econd carboxyl group being part of side chain. D,E
● molecule that has positive charge on one atom and a negative
charge on another atom, but which has no net charge
o The net charge on a zwitterion is zero
ISOELECTRIC POINTS
● This pH value is known as the isoelectric point for the amino acid.
o Is the pH at which an amino acid exists primarily in its
zwitterion form

ESSENTIAL AMINO ACIDS PEPTIDE FORMATION

● standard amino acid needed for protein synthesis ● Formed by a biochemical reaction that extracts a water (H2O)
o R*,H,M,I,L,K,W,T,F,V molecule
▪ R – arginine is essential for children’s growth but not for ● Peptide bond - aka Amide bond - a covalent bond between the
adult carboxyl group of one amino acid and the amino group of another
NON-ESSENTIAL AMINO ACIDS amino acid
● Synthesized by the body ● Peptide – an unbranched chain of amino acids, each joined to the
o C,A,N,D,E,Y,S, Q,G,P next by a peptide bond

1. COMPLETE DIETARY PROTEIN - contains essential amino TYPES OF PEPTIDE BOND

acids in same relative amounts which the body needs
2. INCOMPLETE DIETARY PROTEIN - does not contain adequate 1. Dipeptide - with 2 or more amino acids
amounts, relative to the body’s needs 2. Tripeptide - with 3 or more amino acids joined together in a chain
3. LIMITING AMINO ACID - essential amino acid that is missing, or 3. Oligopeptide - with 10 or 20 amino acid residues present in chain
present in inadequate amounts
4. COMPLEMENTARY DIETARY PROTEINS - When combined, 4. Polypeptide - with longer unbranched chain of amino acids
two or more incomplete dietary proteins provide the organism
with all essential amino acids.
o Ex. Rice and beans servings

USES/FUNCTIONS OF AMINO ACIDS

1. Trp - necessary for the synthesis of neurotransmitter serotonin
o Natural relaxant - helps alleviate insomnia
● Can be metabolized to niacin Vit. B3 if needed
● Used to synthesized melatonin
2. Tyr - precursor of dopamine, norepinephrine, epinephrine
● Promotes healthy thyroid functioning
3. Val, Ile, Leu - enhance energy, increase endurance, aid in
muscle tissue recovery and repair
● lowers elevated blood sugar levels
4. Lys - precursor for L-carathine - essential for healthy nervous
system
● absorption of calcium EXAMPLES OF BIOCHEMICALLY IMPORTANT PEPTIDES:
● bone development in children 1. Oxytocin (9) - Uterus-Contracting Hormone
5. Met - Is antioxidant 2. Vasopression (ADH or antidiuretic hormone) - Enhances
● helps in breakdown of fats and aids in muscle degeneration reabsorption of free water & plays role in Blood pressure control
● Helps lower cholesterol levels 3. Enkephalins (5) - pain killers neuromodulators in the brain and
● Principle supplier of sulfur spinal cord
6. Phe - Beneficial for healthy nervous system. 4. Glutathione (3) - Found in most living cells as antioxidant &
● useful against depression and suppressing appetite promote tissue growth
● produce dopamine and norepinephrine 5. TRH (Thyrotropin Releasing Hormone) (3) - Hypothalmic
7. Ala - removes toxic substances released from breakdown of Neurohormone or TSH or thyroid-stimulating hormone
muscle protein during intensive exercise 6. Angiotensin II (8) - Pressor Agent
8. Cys - antioxidant (free radical scavenger), and has synergetic o increase blood pressure by vasoconstriction.
effect when taken with other antioxidants such as vitamin E and o can also trigger thirst or the desire for salt
selenium 7. Somatostatin (14) - Inhibits Growth Hormone Release
o used to treat ulcers

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8. Bradykinin (9) - Hypotensive Vasodilator (acts on smooth 6. Amphoteric nature - they act both as acids and basis
muscle) 7. Ion binding capacity - proteins can form salts with both cations
9. Endothelin (21) - Potent Vasoconstrictor (structurally similar to and anions based on their net charge
some snake venoms) 8. Solubility - influenced by pH
10. Mellitin (26) - Honey Bee Venom (used to treat rheumatism) o Lowest at isoelectric point and increases with acidity
11. Glucagon (29) - Hyperglycemic Factor (used as an anti-diabetic) 9. Optical activity - all protein solutions rotate the plane of
12. Insulin (51) - Pancreatic Hormone (used in treatment of diabetes) polarized light to the left, these are levorotatory.

STRUCTURES OF PROTEIN CHEMICAL PROPERTIES OF PROTEINS

1. Primary protein structure - sequece of a chain of amino acids
o Held by covalent peptide bonds
2. Secondary protein structure - hdyrogen bonding of the peptide
backbone causes the amino acids to fold into a repeating pattern
o Regular arrangements of amino acids located near to each
other in primary structure
o Other forms:
▪ β-Bends (reverse turn, β -turns)
▪ Nonrepetitive 2nd structure
▪ Supersecondary structures (motifs)
3. Tertiary protein structure - three-dimensional folding pattern of
a protein due to side chain interactions
o Stabilized by: hydrophobic interactions, hydrogen bonds,
electrostatic interactions, disulfide bonds
4. Quaternary protein structure - protein consisting of more than
one amino acid chain
o The arrangement of multiple polypeptide subunits in the
protein
o Stabilized by: hydrophobic interactions, hydrogen bonds,
electrostatic interactions
● Human hemoglobin molecule - a tetramer w/ two alpha and two
beta polypeptide chains
HOW DO PROTEINS ARRIVE AT THEIR FINAL SHAPES?
1. Protein folding - occurs within the cell in seconds to minutes,
involves nonramdom, ordered pathways
2. Denaturation of proteins - results in the unfolding and
disorganization of the protein’s secondary and tertiary structures
3. Role of chaperones in protein folding - information needed for
correct protein folding is contained in the primary structure of the
polypeptide.
o The chaperones - aka heat shock proteins (HSP), interacts
with a polypeptide at various stages during the folding
process.
PHYSICAL PROPERTIES OF PROTEINS
1. Color and taste - colorless and tasteless
o homogeneous and crystalline
2. Shape and size - range in shape from simple crystalloid
spherical structures to long fibrillar structures
3. Molecular weight - generally have large molecular weight
4. Colloidal nature - diffusion rates are extremely slow and
produce considerable light scattering in solution
5. Denaturation - refers to changes in the properties of protein
o Loss of biologic activity
● Hydrolysis - proteins are hydrolyzed by variety of hydrolytic
agents
A. By acidic agents
B. By alkaline agents
● Reactions involving COOH Group
A. Reaction wth alkalies (salt formation)
B. Reactions with alcohols (esterification)
C. Reaction with amines
● Reactions involving NH2 Group
A. Reaction with mineral acids
B. Reaction with formaldehyde
C. Reaction with benzaldehyde
D. Reaction with nitrous acid
E. Reaction with acylating agents
F. Reaction with FDNB or sanger’s reagent
G. Reacttion with dansyl chloride
● Reactions involving both COOH and NH2 Group
A. Reaction with triketohydrindene hydrate
B. Reaction with phenyl isocyanate
C. Reaction with phenyl isothiocyanate
D. Reaction with phosgene
E. Reaction with carbon disulfide
● Reactions involving R-Group or side chain
A. Biuret test - test for proteins with peptide bonds
o Positive reaction blue to violet
B. Xanthoproteic test - detection of amino acids containing
phenolic or indolic groups
o Positive results: orange colored solution presents positive
test
o Negative results: orange colored solution presents negative
test
C. Millon’s test - used for detection of the amino acid tyrosine
o Positive results: red or pink colored precipitate
o Negative results: absence of colored precipitate in the test
tube
D. Sullivan and McCarthy’s test - test for detection of the amino
acid methionine
o Positive results: appearance of red color
o Negative results: absence of red color
E. Sakaguchi test - consisting of colorimetric reaction
o Used as a quantitative test for arginine
o Positive results: formation of red color
o Negative results: absence of red color
F. Pauly test - detection of tyrosine and histidine
o Positive results: apperance of red colored complex
o Negative results: absence of red colored
G. Ehrlich test - used for detection of tryptophan
o Positive results: apperance of red to purple or blue-violet
color
o Negative results: absence of blue-violet color
● Reactions involving SH Group
A. Nitroprusside test: red color develops with sodium
nitroprusside
o The test is specific for cysteine
B. Sullivan test: cysteine develops red color in presence of
sodium
CLASSIFICATION OF PROTEINS
● Proteins are classified based on the number of peptide chain ,
chemical composition, shape and function
NUMBER OF PEPTIDE CHAIN
1. MONOMERIC PROTEIN - one peptide chain is present
o Example: myoglobin
2. MULTIMERIC PROTEIN - more than one peptide chain is present

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o peptide chains present are called protein subunits. ▪ Can be denatured

o Example: insulin

BASED ON CHEMICAL COMPOSITION

1. SIMPLE PROTEIN - only amino acid residues are present
o Examples of Simple protein:
▪ Albumins - (Serum albumin (blood), Lactalbumin
(milk) ,Ovalbumin (eggwhite)
▪ Globulins - (Ovoglobulin (eggwhite), Edestin
(hempseed), Legumin (peas), Myosinogen (muscles),
Serum globulin (blood)
▪ Glutelins - Glutenin (wheat), Oryzenin (rice)
▪ Prolamines - Gliadin (wheat), Zein (corn), Hordein
(barley)
▪ Histones - Thymus histones, Scobrone of Mackerel
▪ Protamines - Salmin (salmon sperm)
▪ Scleroproteins (Albuminoids) - Keratin (epidermal
tissues), Elastins (Ligaments), Collagen (hides, bones
and cartillage)
2. CONJUGATED PROTEIN - one or more non-amino acid entities
present FIBROUS GLOBULAR
● prosthetic group - a non-amino acid group present in a conjugated
protein
water-insoluble Water-soluble
1. Nucleoproteins - Ribosomes, Viruses, Chromatin, Products
from glandular tissues Germ of grains
usually have a single type of secondary several types of secondary
2. Glycoproteins (more proteins less carbohydrates) - Mucin ,
structure structure.
Tendomucoid (tendons), Osseomucoid (bones), gamma
globulin, Interferon (antiviral protection)
3. Phosphoproteins - Casein (milk) Vitellin (egg yolk) generally have structural functions that involved in metabolic
4. Chromoproteins/Hemoproteins - Hemoglobin, Myoglobin, provide support chemistry, performing
Cytochromes, Rhodopsin and external protection, functions such as catalysis,
5. Lipoproteins - Lecithin Cephalin transport, and regulation
6. Metalloproteins - iron–ferritin, zinc–alcohol dehydrogenase Lesser in kind of proteins Greater in kind of proteins

o Examples of Conjugated proteins:

A. Primary Protein derivatives – proteins which have Most abundant in the human body Less
undergone slight intramolecular rearrangement
▪ w/ denatured proteins Greater mass composition Lesser mass composition
1. PROTEANS: Ex: Myosan from myosin, Edestan from
edestin
2. METAPROTEINS: Ex: Acid metaproteins (acid BASED ON FUNCTION
albuminate), Alkali metaproteins (alkali albuminate)
1. Catalytic - biochemical catalyst
3. COAGULATED PROTEINS: Ex: Cooked egg albumin,
o Ex. Enzymes
Cooked meat
2. Defense - Protect body’s immune system/response
B. Secondary Protein derivatives - Product of more
o Ex. Immunoglobulins or antibodies
extensive hydrolysis
3. Transport - carries oxygen from the lungs to other organs and
▪ Exhibit certain common properties such as solubility in
tissues
water
o carries iron from the liver to the bone marrow
1. PRIMARY PROTEOSES - Soluble in water,
o Ex. Hemoglobin, Transferrin
precipitated by conc, Not coagulated by heat
4. Messenger - transmit signals
2. SECONDARY PROTEOSES - Properties
o Ex. Insulin, Glucagon, Human growth hormone
Precipitated only by complete saturation
5. Contractile - necessary for all forms of movement
3. PEPTONES - Not coagulated by heat, Not
o Ex. Actin and myosin
precipitated by saturation
6. Structural - confer stiffness and rigidity to otherwise fluid- like
4. PEPTIDES - combinations of two or more amino
biochemical
acids
o Ex. Collagen, Keratin
▪ Present properties like peptones Ex. di, tri,tera,penta
7. Storage - bind (and store) small molecules for future use
etc.
o Ex. Ferritin, Myoglobin
3. DERIVED PROTEIN - include substances formed from simple
8. Regulatory - Act as sites
conjugated proteins
o Ex. transcription factors (TFs)
9. Transmembrane - function as gateways
BASED ON SHAPE o Ex. Membrane transport proteins
1. FIBROUS - molecules have an elongated shape with one dimension 10. Nutrient - important in the early stages of life, from embryo to infant
o Properties: o Ex. Casein, Ovalbumin
▪ Tend to have simple, regular and linear structures. 11. Buffer - part of the system by which the acid-base balance within
▪ Largely insoluble in ordinary aqueous media body fluids is maintained
▪ Molecular weights are high o Ex. Hemoglobin
▪ Functions is for structural and support 12. Fluid Balance - help maintain fluid balance between blood and
2. GLOBULAR - molecules have peptide chains that are folded into surrounding tissue
spherical shapes o Ex. Albumin, Globulin
o Properties:
▪ Soluble in aqeous media PROTEIN RELATED DISORDERS:
▪ Have been crystallized and have definite molecular
weights

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● Protein Energy (calorie) Malnutrition (PEM): Kwashiorkor & 1. Peptide bond – the strongest bond
Marasmus 2. Disulfide bond - is a covalent bond between two sulfur. Results from
1. Kwashiorkor: occurs when protein deprivation is relatively the oxidation of the –SH (sulfhydryl) groups of two cysteine
greater than calories molecules to form “cystine”
o frequently seen in children after weaning at about one year 3. Hydrogen Bond - result from the attraction of electronegative atoms
of age in the protein molecule. Weaker than the peptide and disulfide bonds.
o Symptoms: stunted growth, edema, skin lesions,
depigmented hair, anorexia, enlarged fatty liver, and
decreased plasma albumin concentration.
o Protein deprivation - associated with severely decreased
synthesis of visceral protein (usually albumin)

2. Marasmus: occurs when calorie deprivation is relatively greater

than protein
o usually occurs in children younger than 1 year of age when
breast milk
o Symptoms: arrested growth, extreme muscle wasting
(emaciation), weakness, and anemia

● Protein misfolding: Amyloidosis, Prion disease (human, sheep,

cow)
1. Amyloidosis: accumulation of insoluble, long, fibrillar protein
assemblies consisting of β-pleated sheets caused by abnormal
proteolytic cleavage.
2. Prion disease: The prion protein (PrP or PRNP) has been
strongly implicated as the causative agent of transmissible
spongiform encephalopathies (TSEs)
● Hemoglobinopathies
o Synthesis of structurally abnormal hemoglobins
o Synthesis of insufficient quantities of normal hemoglobin
● Collagenopathies - deposition of insoluble fibers outside the cell
● Alpha-1-Antitrypsin Deficiency

● Examples of PROTEINS
o HORMONES = messengers
o ENZYMES = speed up reactions
o CELL RECEPTORS = “antinnae”
o ANTIBODIES = fight foreign invaders
o MEMBRANE CHANNELS = allowing specific molecules to
enter or leave a cell

● Bonding in proteins

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