PROTEINS

CHARACTERISTICS OF PROTEINS
- has carbon, hydrogen, oxygen, and nitrogen (many has also sulfur)
- monomer units: amino acids
AMINO ACIDS: THE BUILDING BLOCKS FOR PROTEINS

- has both an amino group (-NH2) and a carboxyl group (-COOH)

- alpha-amino acid
o always found in proteins
o carboxyl group is attached to an alpha-carbon atom
- 20 STANDARD AMINO ACIDS
Nonpolar
 hydrophobic
 1 amino, 1 carboxyl, 1 nonpolar side chain
 inside the proteins
o Glycine (Gly, G)
o Alanine (Ala, A)
o Valine (Val, V)
o Leucine (Leu, L)
o Isoleucine (Ile, I)
o Proline (Pro, P)
o Phenylalanine (Phe, F)
o Methionine (Met, M)
o Tryptophan (Trp, W)
Polar Neutral
 1 amino, 1 carboxyl, 1 polar but neutral side chain
 R group can hydrogen-bond to water
 neither positively charged nor negatively charged
o Serine (Ser, S)
o Cysteine (Cys, C)
o Threonine (Thr, T)
o Asparagine (Asn, N)
o Glutamine (Gln, Q)
o Tyrosine (Tyr, Y)
Polar Acidic
 1 amino, 2 carboxyls, 2nd carboxyl is part of the side chain
 side chain is negatively charged
o Aspartic Acid (Asp, D)
o Glutamic Acid (Glu, E)
Polar Basic
 2 amino, 1 carboxyl, 2nd amino is part of the side chain
 side chain is positively charged
o Histidine (His, H)
o Lysine (Lys, K)
o Arginine (Arg, R)
MTCHM 3- Medical Biochemistry Proteins MAHAL C. BARROSO
ESSENTIAL AMINO ACIDS
Arginine (essential for infants/children not for adults) Methionine
Histidine Phenylalanine
Isoleucine Threonine
Leucine Tryptophan
Lysine Valine

- Complete dietary protein

o all essential amino acids in an adequate amount
o source: meat, fish, and eggs
- Incomplete dietary protein
o doesn’t have an adequate amount of fatty acids
o limiting amino acid: an essential amino acid that is missing, or only present in
inadequate amounts
o tryptophan in gelatin & lysine, methionine, and tryptophan in plant sources
- Complementary dietary proteins
o 2 or more incomplete DP that when combined, provide adequate protein
ACID-BASE PROPERTIES OF AMINO ACIDS
- Zwitterion
o molecule that has (+) atom and negatively (-) atom but has 0 net charge
o acidic solution: zwitterions become (+) ion
o basic solution: zwitterions become (-) ion
- amino acid solutions and proteins can function as buffers
- Isoelectric Points
o pH of an amino acid in zwitterion form
o 15/20 amino acids have an isoelectric point of 4.8-6.3
CYSTEINE: A CHEMICALLY UNIQUE AMINO ACID
- only standard essential amino acid that has a side chain containing sulfhydryl group (-SH)
- Cystine- has 2 cysteine residues linked by disulfide bonds
PEPTIDES

- Dipeptide: 2 amino acids

- Tripeptide: 3 amino acids
- Oligopeptide: 10-20 amino acids
- Peptide bond
o Covalent bond that links amino acids
o Bond between the carboxyl group of one amino acid and the amino group of another
amino acid

MTCHM 3- Medical Biochemistry Proteins MAHAL C. BARROSO

BIOCHEMICALLY IMPORTANT SMALL PEPTIDES
SMALL PEPTIDE HORMONES
1. Oxytocin
- produced by the pituitary gland
- nonapeptide (9 amino acids)
- regulate uterine contraction and lactation
2. Vasopressin
- regulates the excretion of water by the kidneys
- affects BP
SMALL PEPTIDE NEUROTRANSMITTERS

1. Enkephalins
- pentapeptide (5 AA)
- produced by the brain that bind at receptor sites in the brain to reduce pain
o Met-enkephalin: Tyr-Gly-Gly-Phe-Met
o Leu-enkephalin: Tyr-Gly-Gly-Phe- Leu
SMALL PEPTIDE ANTIOXIDANTS

1. Glutathione
- tripeptide (3 AA; Glu-Cys-Gly)
- present in most cells
- regulator of oxidation-reduction reactions
- antioxidant that protects cellular contents from oxidizing agents
GENERAL STRUCTURAL CHARACTERISTICS OF PROTEINS
Protein- a peptide that has at least 40 amino acid residues
CLASSIFICATIONS:

- Based on PEPTIDE CHAIN

o Monomeric Protein- has 1 peptide chain
o Multimeric Protein- has more than 1 peptide chain
- Based on CHEMICAL COMPOSITION
o Simple Protein- only 1 amino acid residue is present
o Conjugated Protein- has 1 or more non-amino-acid entities present in addition to one
or more peptide chains
 Lipoproteins- lipid prosthetic group
 Glycoproteins- carbohydrate prosthetic group
 Metalloproteins- metal ion prosthetic group
 Hemoproteins- heme unit prosthetic group
 Phosphoproteins- phosphate prosthetic group
 Nucleoproteins- nucleic acid prosthetic group
o Prosthetic Group- a non-amino-acid group present in a conjugated protein

MTCHM 3- Medical Biochemistry Proteins MAHAL C. BARROSO

STRUCTURE OF PROTEINS
PRIMARY STRUCTURE

- order of attachment of amino acids linked together in a protein

- primary structure of a specific protein is always the same regardless of where the protein is
found within an organism
SECONDARY STRUCTURE

- arrangement in space adopted by the backbone portion of a protein

- hydrogen bonding between carbonyl and amino group in a peptide linkage is responsible for
the secondary structure

Alpha Helix Beta Pleated Sheet Unstructured Segments

- single protein chain
adopts a shape that
resembles a coiled
spring
- two fully extended - protein secondary
protein chain segments structure that is neither
in the same or different an alpha helix nor beta
molecules are held pleated sheet
together by hydrogen
bonds

*Note: It is possible for a protein to have both alpha helix and beta pleated sheet
TERTIARY STRUCTURE

- the overall 3-dimensional shape of a protein that results from the interactions between amino
acid side chains (N groups) that are widely separated from each other within a peptide chain
- INTERACTIONS RESPONSIBLE:
o Covalent Disulfide Bonds
o Electrostatic Attractions
o Hydrogen Bonds
o Hydrophobic Attractions
QUATERNARY STRUCTURE

- highest level of protein organization

- only found in multimeric proteins
- organization among various peptide subunits in a multimeric protein
- INTERACTIONS RESPONSIBLE:
o Electrostatic Attractions
o Hydrogen Bonds
o Hydrophobic Interactions
PROTEIN HYDROLYSIS
Complete Incomplete
o break all peptide bonds o not all peptide bonds are broken
o product: free amino acids o product: free amino acids + small
peptides

MTCHM 3- Medical Biochemistry Proteins MAHAL C. BARROSO

PROTEIN DENATURATION
- partial or complete disorganization of a protein’s characteristic 3-dimensional shape as a result
of disruption of its secondary, tertiary, and quaternary structural interactions
- does not affect the primary structure of a protein
- Renaturation: limited denaturation
- Coagulation: precipitation of denatured protein
- Cauterization: sealing of small blood vessels in surgery
*Note: 70% alcohol is more effective than pure isopropyl or ethyl alcohol

PROTEIN CLASSIFICATION BASED ON SHAPE

1. FIBROUS PROTEIN 2. GLOBULAR PROTEIN
- water insoluble
- has an elongated shape
molecule
- has a tendency to
aggregate to form
macromolecular structure
- e.g.
 keratins in fingernails
 collagens in tendons,
bones, and other
connective tissue
 elastins in blood vessels
and ligaments
 myosins in muscle tissue
 fibrin in blood clots
3. MEMBRANE PROTEIN
- has spherical/globular - associated with a
shape molecule membrane system
- e.g. of a cell
 insulin: a hormone that
controls glucose
metabolism
 myoglobin: oxygen
storage in muscles
 hemoglobin: oxygen
transport in blood
 transferrin: iron transport
in blood
 immunoglobulins:
immune system response

MTCHM 3- Medical Biochemistry Proteins MAHAL C. BARROSO

PROTEIN CLASSIFICATION BASED ON FUNCTION
1. Catalytic Proteins
- Enzymes= catalytic action
2. Defense Proteins
- Immunoglobulins/antibody= immune response
3. Transport Proteins
- Hemoglobin: carries O2 from lungs to other tissues and organs
- Transferrin: carries Fe from the liver to the bone marrow
- LDL, HDL: carries cholesterol in the bloodstream
4. Messenger Proteins
- Insulin
- Glucagon
- Human Growth Hormone
5. Contractile Proteins
- Actin: for cell movement
- Myosin: for cell movement
6. Structural Proteins
- Collagen: component of cartilage
- alpha-Keratin: fingernails
7. Transmembrane Proteins
- controls movement of small molecules or ions through the cell membrane
8. Storage Proteins
- Ferritin: iron storage in the cell
- Myoglobin: oxygen storage in muscle
9. Regulatory Proteins
- control enzymatic actions
10. Nutrient Proteins
- Casein: in milk
- Ovalbumin: in egg-white
11. Buffer Proteins
- Hemoglobin
12. Fluid Balance Proteins
- Albumin: responsible for osmotic pressure in blood vessels
- Globulin: responsible for osmotic pressure in blood vessels

MTCHM 3- Medical Biochemistry Proteins MAHAL C. BARROSO