1.3 - Proteins Flashcards
Draw the general structure of an amino acid
What is the bond formed between 2 amino acids in a condensation reaction?
peptide bond
between amine and carboxyl groups
How is a dipeptide formed?
condensation of 2 amino acids
How is a polypeptide formed?
condensation of many amino acids
3 types of bond that contribute to the tertiary structure of a protein (shape)
- hydrogen bonds
- ionic bonds
- disulfide bridges
Describe the primary structure of a protein
amino acid sequence
Describe the secondary structure of a protein
2D folding of polypeptide chain as a result of H bonding
e.g beta-pleated sheet, alpha helix
Describe the tertiary structure of a protein
3D folding of a polypeptide chain due to interactions between R groups
Describe the quaternary structure of a protein
multiple polypeptide chains
Describe the Biuret test for proteins
- add Biuret
- positive: blue -> lilac
How does an enzyme increase rate of reaction?
- lowers activation energy
- induced fit causes active site to change shape
- ESC complex causes bonds to weaken as they bend (and break)
Describe the induced fit model of enzyme action
- substrate binds to active site, forming ESC
- active site changes shape to now complementary to substrate
- (H) bonds are broken and formed in substrate
Why are enzymes referred to as specific?
specific tertiary structure (active site) which is complementary to a specific substrate
Describe the effect of enzyme concentration on the rate of reaction
increasing enzyme concentration increases the rate of reaction
Describe the effect of substrate concentration on the rate of reaction
as substrate conc increases rate of reaction increases, until it plateaus due to other limiting factor e.g enzyme conc