Unit 1- Amino Acids, Proteins, and Enzymes Flashcards
Amino Acid Features
Amino group, carboxyl group, variable R group.
Protein Functions
Catalysis, structure, transport, signaling.
Amino Acid Structures
Amino group, central carbon, carboxyl group, R group.
Hydrophobic vs. Hydrophilic amino acids
Hydrophobic: Nonpolar side chains.
Hydrophilic: Polar or charged side chains
Bond holding amino acids together
Peptide bonds (between amino group an carboxyl group).
Protein Structures
Primary: Sequence of amino acids.
Secondary: Alpha helices, beta sheets (hydrogen bonds).
Tertiary: 3D folding.
Quaternary: Multiple polypeptides.
Prion
Misfolded protein causing other proteins to misfold.
IDPs and IDRs
Intrinsically Disordered Proteins/Regions, flexible, involved in diverse functions.
Enzyme Importance
Catalyze biochemical reactions, increase reaction rates
Catalyst Properties
- Lower activation energy.
- Increase reaction rate.
Enzyme Action
Lowers activation energy, stabilizes transition state.
Models of enzyme function
Lock and Key: Active site fits substrate.
Induced Fit: Enzyme changes shape to fit substrate.
Cofactors
Inorganic: Metal ions.
Organic (coenzymes): Vitamins, help enzyme function.
Allosteric regulation
Regulation by binding at a site other than the active site.
Feedback Inhibition
Product inhibits an earlier step in the pathway.
