ACS Biochemistry Final questions with verified answers
1) competitive inhibitors
2) uncompetitive inhibitors
3) mixed inhibitors
(chapter 6) Ans✓✓✓ 1) Km increases, no effect on Vmax, same y-intercept,
increasing slope, increased substrate can overcome
2) Vmax decreases, y-intercepts increase, constant slope, increased substrate
cannot overcome
3) Km increases, Vmax decreases, y-intercepts increase, slope increases, increased
substrate cannot overcome
2,3-bisphosphoglycerate (5) Ans✓✓✓ decreases affinity of Hb for O2, stabilizing
T-state
Acid Dissasociation constant Ka (2) Ans✓✓✓ quantitative measure of the
strength of an acid in solution
activity (3) Ans✓✓✓ total units of a certain enzyme in a solution
Affinity chromatography (3) Ans✓✓✓ based on the binding affinity of a protein.
The beads in the column have a covalently attached chemical group. A protein
with affinity for this particular chemical group will bind to the beads in the
column, and its migration will be retarded as a result
amylose chain (20) Ans✓✓✓ α-1,4-linkages that produce a coiled helix similar to
an α-helix. has a reducing end and a non-reducing end
, anomeric carbon (20) Ans✓✓✓ carbon that is cyclized. always the same as the
aldo or keto carbon in the linear form.
antibodies or immunoglobulins, Ig (chapter 5) Ans✓✓✓ bind bacteria, viruses, or
large molecules identified as foreign and target them for destruction
Bohr effect (5) Ans✓✓✓ effect of H+ and CO2 on the binding and release of O2
from Hb. O2 binds well at higher pH and low CO2.
carnitine shuttle (17, p. 634) Ans✓✓✓ transports free fatty acids across inner
mitochondrial membrane. 3 enzymatic reactions:
1) esterification to CoA (acyl CoA synthetases)
2) transesterification to carnitine (folllowed by transport)
3) transesterification back to CoA
cation-exchange chromatography (3) Ans✓✓✓ solid matrix (stationary phase)
has negatively charged groups. In the mobile phase, proteins with a net positive
charge migrate through the matrix more slowly than those with a net negative
charge. The two types of protein can separate into two distinct bands.
chaperonins (4) Ans✓✓✓ elaborite protein complexes required for the folding of
a number of cellular proteins that do not fold spontaneously
chymotrypsin (6) Ans✓✓✓ cleaves proteins on C-terminal end of Phe, Trp, and
Tyr
1) competitive inhibitors
2) uncompetitive inhibitors
3) mixed inhibitors
(chapter 6) Ans✓✓✓ 1) Km increases, no effect on Vmax, same y-intercept,
increasing slope, increased substrate can overcome
2) Vmax decreases, y-intercepts increase, constant slope, increased substrate
cannot overcome
3) Km increases, Vmax decreases, y-intercepts increase, slope increases, increased
substrate cannot overcome
2,3-bisphosphoglycerate (5) Ans✓✓✓ decreases affinity of Hb for O2, stabilizing
T-state
Acid Dissasociation constant Ka (2) Ans✓✓✓ quantitative measure of the
strength of an acid in solution
activity (3) Ans✓✓✓ total units of a certain enzyme in a solution
Affinity chromatography (3) Ans✓✓✓ based on the binding affinity of a protein.
The beads in the column have a covalently attached chemical group. A protein
with affinity for this particular chemical group will bind to the beads in the
column, and its migration will be retarded as a result
amylose chain (20) Ans✓✓✓ α-1,4-linkages that produce a coiled helix similar to
an α-helix. has a reducing end and a non-reducing end
, anomeric carbon (20) Ans✓✓✓ carbon that is cyclized. always the same as the
aldo or keto carbon in the linear form.
antibodies or immunoglobulins, Ig (chapter 5) Ans✓✓✓ bind bacteria, viruses, or
large molecules identified as foreign and target them for destruction
Bohr effect (5) Ans✓✓✓ effect of H+ and CO2 on the binding and release of O2
from Hb. O2 binds well at higher pH and low CO2.
carnitine shuttle (17, p. 634) Ans✓✓✓ transports free fatty acids across inner
mitochondrial membrane. 3 enzymatic reactions:
1) esterification to CoA (acyl CoA synthetases)
2) transesterification to carnitine (folllowed by transport)
3) transesterification back to CoA
cation-exchange chromatography (3) Ans✓✓✓ solid matrix (stationary phase)
has negatively charged groups. In the mobile phase, proteins with a net positive
charge migrate through the matrix more slowly than those with a net negative
charge. The two types of protein can separate into two distinct bands.
chaperonins (4) Ans✓✓✓ elaborite protein complexes required for the folding of
a number of cellular proteins that do not fold spontaneously
chymotrypsin (6) Ans✓✓✓ cleaves proteins on C-terminal end of Phe, Trp, and
Tyr
