Integration and Synthesis of Proteins and Enzymes Flashcards
The basic unit of a living organism
Cell
Biochemical features of living organisms
Proteins, nucleic acids, carbohydrates, and lipids
A bond that links protein polymer(s) of an amino acid
Peptide Bonds
Functions of proteins
Structure (cytoskeleton), catalysis (enzymes), locomotion (actin and myosin), protection (antibodies), cellular communication (receptors), transport (hemoglobin and channels), storage (myoglobin), and energy source.
Hydrophobic amino acids
Glycine, Alanine, Valine, Leucine, Isoleucine, Proline, Methionine, Phenylanaline, and Tryptophan
Polar uncharged amino acids
Cysteine, Serine, Threonine, Tyrosine, Asparagine, and Glutamine
Polar charged amino acids
Aspartic acid, Glutamic acid, Histidine, Lysine, and Arginine
Primary protein organization
Sequence of amino acids from N-terminus to C-terminus
Secondary protein organization
Intramolecular H-bonding in the amino acid skeleton and the existence of spagial arrangement: a-helix, B-sheet, and random coil
Tertiary protein organization
3D organization of polypeptide chains and contains intramolecular bonding between R-groups
Intramolecular bonding under tertiary protein organization
Disulfide bonds, H-bonding, Electrostatic, Hydrophobic interaction, and Metal ion complexation.
Quaternary protein arrangement
Arrangement of sub-units (polypeptide chains) in the complex protein
Sample proteins
Hemoglobin and myoglobin, insulin and glucagon, and immunoglobulin
Denaturation
Destruction of protein structure causing loss of enzyme activity
Denaturing agents
Heat, chaotropic agents (urea, alcohol, detergent), and reducing agents (mercaptoethanol)
These are polymers of amino acids
Proteins
These are chemical groups attached to an a-carbon
Amino group, carboxyl group, and side chain group (R)
All amino acids have at least one chiral center, except for?
Glycine
Two stereoisomers
L and D-Amino acid
Majority of amino acids are in what configuration?
L-configuration
Molecules that contain both positive and negative chargesa
Zwitterion
Bronsted Acid
Proton donator
Bronsted Base
Proton acceptor
This yields the different ionisation states of amino acids
Titration of amino acids
The pH at which the net charge of an amino acid or peptide is zero
Isoelectric pH (pI)
Amide bond between an a-carboxyl group of one amino acid and the a-amino group of another acid
Peptide bond
This aids in the linkage of two or more amino acids
Peptide bonds
Peptide direction
From N-terminus (free amino group) to C-terminus (free carboxyl group)