Unit 4 Flashcards
________ structure level of proteins: order of amino acids.
Primary
_________ structure level of proteins: small spirals or kinks.
Secondary
______ structure level of proteins: polypeptide folds into globular structure.
Tertiary
________ structure level of proteins: combination of multiple polypeptides
Quaternary
not all proteins have every level, many lack _____ and _______.
Tertiary and Quaternary
- Guide proper folding.
- Reduce aggregation.
Chaperonin
______ of proteins can lead to disease and allergies.
misfolding
_______ is when a protein unfolds and loses its secondary, tertiary, quaternary structure.
Denaturation
how can cells use denaturation
to turn proteins on or off
Biological catalysts
Enzymes
long chain of amino acids linked by peptide (covalent) bonds
Polypeptides
determines the amino acid’s nature (that is, whether it is acidic, basic, polar, or nonpolar)
Side Chain or R group
energy necessary for a reaction to occur
Activation energy
Molecule on which enzymes act
substrate
the region of an enzyme where a substrate binds
Active site
Molecule that activates enzymes
Cofactor
What are the two types of cofactors?
o Inorganic cations
o Coenzymes = organic molecules (often vitamins)
molecule that inactivates enzyme.
Inhibitor
______ inhibitors bind at active site and blocks active site
competitive
______ inhibitors bind away from active site. – change shape of active site.
non-competitive
molecule increases or decreases enzyme activity by binding away from active site.
allosteric regulator
