a.It is a powerful method to determine the 3-dimensional structure of proteins.
b.Large amount of protein sample is needed for mass spectrum, and thus it is very expensive.
c.It can be sued for protein location in a living cell.
d. It can be used to measure the molecular weight of proteins.
e.It can be used to determine the stability of a protein structure in solution.
2. In the alpha-helices, which of the following statement is true?
a.Hydrogen bonds are almost perpendicular to the helix axis.
b.Backbone carbonyl oxygen residue (i) hydrogen bonds to backbone NH of the fourth residue
of chain of residue (i + 4).
c. The rise or advance per amino acid residue is 0.54 nm.
d.Side chains point inward from an α-helix, i.e. buried inside.
e.The pitch or advance per turn is 0.15 nm.
3. An inhibitor binds enzyme or ES complex other than at the catalytic site, and substrate
binding is unaltered, but ESI complex cannot form products. What type of inhibitor this is?
a.An uncompetitive inhibitor
b.A noncompetitive inhibitor
c.An irreversible inhibitor
d.A competitive inhibitor
4. Which property is NOT true concerning enzymes and chemical catalysts?
a.Enzymes can be regulated, and normally chemical catalysts cannot.
b.Enzymes can act in milder conditions, but chemical catalysts normally cannot.
c.Both enzymes and chemical catalysts can increase the rate of chemical reactions.
d.Both enzymes and chemical catalysts can increase the reaction rate by millions to billions of
folds.
e.Both enzymes and chemical catalysts can be recovered unchanged at the end of the
reaction.
5. Which of the following residues CAN be glycosylated?
a.Ala
b.Cys
c.Ser
d.Gln
e.Pro
6. Chymotrypsin belongs to which group of the following enzymes?
a.Hydrolases
b.Transferases
c.Lyases
d.Isomerases
e.Ligases
7. The alpha-helix is formed mainly by
a.side chain-side chain interaction
b.hydrophilic interaction
c.hydrogen bonding
d.disul de bonding
e.hydrophobic interaction
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