Peptide bonds link amino acids: Primary structure.
Amino acid sequence is organized: Still primary structure.
Disulfide bonds are formed between R groups: Tertiary structure.
Alpha and beta helixes are formed: Secondary structure.
Hydrogen bonds are formed: Secondary structure.
Unequal electron clouds in R group: Contributes to tertiary structure.
Charged R groups are developed: Part of the primary structure.
Nonpolar bonding is formed: Contributes to the tertiary structure. Function is determined at multiple levels, mainly tertiary and quaternary structures.
**Function is primarily determined at the quaternary structure, involving multiple protein subunits.
Questions:
What is an allosteric site? It's a spot on a protein (often an enzyme) that can change how the protein works when a molecule binds to it.
How does pH denature enzyme function? Enzymes work best at a specific pH. If the pH is too high or too low, it can change the charges on the enzyme's parts, causing it to lose its shape and function.
Discuss how an inhibitor works. Inhibitors are like stop signs for enzymes. They can either mimic the enzyme's target (competitive) or attach to a different part of the enzyme (non-competitive) to slow down or stop the enzyme's function.
Discuss coenzymes and cofactors. Coenzymes are organic helpers (like vitamins), and cofactors are inorganic helpers (like metal ions). They assist enzymes in their work, like carrying molecules or assisting in chemical reactions.