5. Compare fibroud proteins such as keratin and globular proteins:
a) Water solubility
b) flexible secondary structure
c) highly repetitive primary structure
d) size and ability to associate into larger structures
Give this one a try later!
, a) fibrous: insoluble
globular: soluble
b) fibrous: no
globular: yes
c) fibrous: yes
globular: not necessarily
d) fibrous: elongated structrue; two alpha keratin polypeptides, each of
which form an alpha helix, twisting around each other to form a left-handed
coil
globular: varies
18. Draw an example of a blunt and sticky restriction enzyme cut site.
Give this one a try later!
ACGTGA
A|CGTGA (sticky)
ACG|TGA (blunt)
13.
a) in DNA, which bases hydrogen bond?
b) in each base pair, how many hydrogen bonds are there?
c) which would require higher temp to destroy (melt) the hydrogen bonds?
d) calculate the % A, G, T,C content of each of the following DNA sequences
(complementary strand not shown)
A) ATATATATGC
B) GGCTTAAATT
C) GCGCGCGCTA
D) TTTAAAATGC
e) based on your answer to "d", which would have the highest MP?
Give this one a try later!
, a) A to T and G to C
b) A double bonds to T
G double bonds to C
c) GC
d) A) A=40, T=40, G=10, C=10
B) A= 30, T=40, G=20, C=10
C) A=10, T=10, G=40, C=40
D) A=40, T=40, G=10, C=10
e) C because it has the highest GC content
12. Arginase is part of the urea cycle, catalyzing the hydrolysis of arginine to urea and
ornithine. It is also a target for drug development. It is thought that inhibiting it might
be a treatment for asthma. Two transitions state inhibitors are shown (see skematic)
a) what is a transition state inhibitor (how does its structure compare to the enzyme
substrate? how does its affinity for the enzyme compare to the enzyme's substrate?)?
b) Would it be advantageous for these potential drugs to covalently bind to the
enzyme? why/why not?
c) from a practical standpoint, would it be advantageous for these potential drugs to
be less chemically stable than the substrate?
Give this one a try later!
a) similar to the substrate; binds to the active site with greater affinity than
the substrate
b) not advantageous because the urea cycle would shut down
c) no, because shelf life and time to reach target
25. a) State whether the following reactions occur during stage 1 or 2 of glycolysis
A) NADH formed
B) the aldolase reaction
C) 3-PG formed
D) F6P formed
b) put reactions in order
a) Water solubility
b) flexible secondary structure
c) highly repetitive primary structure
d) size and ability to associate into larger structures
Give this one a try later!
, a) fibrous: insoluble
globular: soluble
b) fibrous: no
globular: yes
c) fibrous: yes
globular: not necessarily
d) fibrous: elongated structrue; two alpha keratin polypeptides, each of
which form an alpha helix, twisting around each other to form a left-handed
coil
globular: varies
18. Draw an example of a blunt and sticky restriction enzyme cut site.
Give this one a try later!
ACGTGA
A|CGTGA (sticky)
ACG|TGA (blunt)
13.
a) in DNA, which bases hydrogen bond?
b) in each base pair, how many hydrogen bonds are there?
c) which would require higher temp to destroy (melt) the hydrogen bonds?
d) calculate the % A, G, T,C content of each of the following DNA sequences
(complementary strand not shown)
A) ATATATATGC
B) GGCTTAAATT
C) GCGCGCGCTA
D) TTTAAAATGC
e) based on your answer to "d", which would have the highest MP?
Give this one a try later!
, a) A to T and G to C
b) A double bonds to T
G double bonds to C
c) GC
d) A) A=40, T=40, G=10, C=10
B) A= 30, T=40, G=20, C=10
C) A=10, T=10, G=40, C=40
D) A=40, T=40, G=10, C=10
e) C because it has the highest GC content
12. Arginase is part of the urea cycle, catalyzing the hydrolysis of arginine to urea and
ornithine. It is also a target for drug development. It is thought that inhibiting it might
be a treatment for asthma. Two transitions state inhibitors are shown (see skematic)
a) what is a transition state inhibitor (how does its structure compare to the enzyme
substrate? how does its affinity for the enzyme compare to the enzyme's substrate?)?
b) Would it be advantageous for these potential drugs to covalently bind to the
enzyme? why/why not?
c) from a practical standpoint, would it be advantageous for these potential drugs to
be less chemically stable than the substrate?
Give this one a try later!
a) similar to the substrate; binds to the active site with greater affinity than
the substrate
b) not advantageous because the urea cycle would shut down
c) no, because shelf life and time to reach target
25. a) State whether the following reactions occur during stage 1 or 2 of glycolysis
A) NADH formed
B) the aldolase reaction
C) 3-PG formed
D) F6P formed
b) put reactions in order
