Ch 5 - Pt 2 - Proteins Flashcards
Enzyme
Proteins that serve as catalysts in living organisms; typically very large molecules that bring together/break apart substrates (the molecules upon which a chemical reaction occurs).
Catalyst
A substance that accelerates the rate if a chemical reaction without affecting the products of the reaction and without itself being altered or consumed by the reaction.
Amino acids
An organic molecule possessing both an amino acid and a carboxyl group.
The monomer building blocks of proteins.
Polypeptides
Polymers of amino acids
A protein consists of one or more polypeptides
Amino acid monomers
Organic molecules possessing both carboxyl and amino groups. Differ in their properties due to differing side chains (R-groups).
How many different amino acid monomers from which polypeptides are assembled?
20
Peptide bonds
The covalent bond between the carboxyl group of one amino acid and the amino group on another formed by a dehydration reaction.
The link between amino acids.
Dehydration reaction.
How are peptide bonds formed?
Through dehydration reactions.
How does a protein’s specific conformation/3D shape effect it’s function?
A protein’s specific conformation determines its function
What are some examples of models depicting a proteins specific conformation (3D shape)?
Space-filling model, ribbon model, 3D complementarity between an antibody protein and an invading virus particle
What are the 4 levels in protein structure?
Primary, secondary, tertiary, and (in some cases) quaternary structure
Primary structure of a protein
1) The linked series of amino acids with a unique sequence.
2) The 29 amino acids can be assembled into 20^127 sequences.
3) Primary structure dictates structure at higher levels.
Secondary structure of proteins
Hydrogen bonds between amino acids of a single polypeptide (a helix) or amino acids of adjacent polypeptides (B sheet) bring about secondary structure
Tertiary structure if proteins
1) Results from interactions between the side chains (R-groups) of amino acids
2) Involves a variety of bonds: disulfide bridges, hydrogen bonds, van der Waals interactions, ionic bonds
Quaternary structure of proteins
Are comprised of 1+ polypeptide subunits