.
5.40
7.15
10.73
12.48
1.82
9.83
11.46
5.51
10.46
12.48
7.95
11.17
4.97
7.0
3.03
It contains hydroxylated amino acids.
One single polypeptide forms a left-handed helix.
Cross-links between neighbouring hydroxylated Lys residues stabilize the helix.
Glycine at every third position is essential for the stability of the triple helical structure.
The triple helical structure twists in the right-handed direction.
With fewer BPG molecules bound there are more heme residues available for O2 binding
Decreased BPG binding biases the fetal hemoglobin toward the T state
More free BPG is available to bind to adult hemoglobin, resulting in a shift of adult hemoglobin to the R state
BPG is available to bind to fetal myoglobin, helping to release O2 in fetal muscle tissue
It reduces fetal hemoglobin's P50
Thrombin
Factor XIa
Factor IXa
Tissue factor
Factor VIIa
Competitive
Noncompetitive
Uncompetitive
Reversible
Irreversible
Figure 10 with alpha = alpha'
Figure 9
Figure 8 with alpha = 2
Figure 8
Figure 9 with alpha' = 2
Ping-pong mechanism
Second order reaction mechanism
Hills reaction mechanism
Allosteric activation mechanism
Random mechanism
Adenosine
Inosine
1,6 Dihydroinosine
Malonate
PCNA
Adenosine
Inosine
1,6 Dihydroinosine
Malonate
PCNA
Figure 6
Figure 7
None of the rest
Figure 9
Figure 10
Figure 5
Figure 7
Figure 9
Figure 10
None of the rest
Figure 10
Figure 5
Figure 6
Figure 8
None of the rest
Km decreases because the inhibitor binds to ES to form ESI which decreases ES
Km unchanged; inhibitor binding does not affect S binding
Km increases because the inhibitor is decreasing the probability of the substrate's binding to the active site
Km increases because the inhibitor binds to ES to form ESI which decreases ES
None of the rest
Km is the [S] at which V0 = 0.5 Vmax
The shape of the curve is a hyperbola.
The y-axis is initial reaction velocity
As [S] increases, the initial velocity of reaction, V0, also increases.
At very high [S], the velocity curve becomes a horizontal line that intersects the y-axis at Km.
Competitive
Allosteric
Dephosphorylating
Co-structural
Dissociative
Its linking number is not changed
The change in its writhing number is 55
Its original linking number is 400
The change in its twist is -55
All answers are correct
Decreases
Increases
Remains the same
Cannot be calculated without knowing the size of the plasmid
None of the answers
The replication machinery is stationary and the template DNA is reeled through it.
The replication machinery move along the template DNA like a train on tracks.
Positive supercoiling facilitates initiation of DNA replication.
Introduction of negative supercoiling to DNA by helicase is dependent on ATP hydrolysis.
Introduction of negative supercoiling to DNA by helicase is independent on ATP hydrolysis.
Adenosine
Inosine
1,6 Dihydroinosine
Malonate
PCNA
The 3'O atoms, enhance
The 2'O atoms, enhance
The 3'O atoms, reduce
The 2'O atoms, reduce
The phosphates, enhance
Telomerase adds DNA sequence repeats to the 5’ end of the DNA strands in the telomere regions
Telomerase joins Okazaki fragments on the lagging strand
In the circular chromosomes of bacteria, DNA replication begins at multiple origins
In prokaryotes DNA ligase is activated by ATP
In eukaryotes DNA ligase is activated by ATP
A G:C base pair will become an A:T base pair
An A:T base pair will become a G:C base pair
A G:C base pair will become a U:T base pair
An A:T base pair will become a U:T base pair
There will be no change seen in the individual's DNA
Lysine, Arginine
Arginine, Leucine
Uracil, Thymine
Glycine, Proline
Glutamate, Aspartate
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