1A: Amino Acids and Proteins

Question 1

What is the difference between noncompetitive and uncompetitive inhibition?

Answer 1

noncompetitive-bind before E-S attach

uncompetitive-bind after formation of E-S complex

Question 2

Which amino acid residues are most prone to phosphorylation?

Answer 2

Serine (S), Threonine (T), and Tyrosine (Y)

Question 3

When do zero-order reactions take place?

Answer 3

enzyme is saturated, [reactant] far exceeds available active sites on enzymes
-catalysis is rate-limiting step

Question 4

What effect do denaturing, reducing, and native have on gel electrophoresis?

Answer 4

denature-disrupt interactions between monomers
reducing-disrupt disulfide bonds
native-keeps original length

Question 5

Which type of inhibitor binds equally to enzyme and enzyme-substrate complex?

Answer 5

noncompetitive inhibitor

Question 6

Which amino acids contain two nitrogen atoms?

Answer 6

asparagine, glutamine, and tryptophan

Question 7

Enzyme catalyze hydrolysis of fats and other carboxylic acid esters

Answer 7

lipases

Question 8

How does SDS-PAGE separate proteins?

Answer 8

based on mass