Question-31.
Arg-->Glu this conversion will affect the structure of the
protein as Arginine is positively charged basic amino acid and
glutamic acid is negatively charged acidic amino acid.
Question 35
Option-2
A is a competative inhibitior of the enzyme and B is the
non-competitive inhibitor of the enzyme. Therefore increasing the
substrate concentration will lower the inhibitory effects of
inhibitor A.
Question-37.
Option 3.
Trypsin cleaves the peptide bond between the carboxy group of
lysine or arginine and the amino group of the adjacent amino acid.
Therefore the three fragments will be
Asp-Leu-Gln-Arg
Ile-Ala-Met-Trp-Phe-Lys
Gln-Met-Asp-Arg
Question 39.
Option 4.
Hexokinase has higher affinity for glucose than glucokinase. But
hexokinase is negatively regulated by Glucose-6-phosphate.
Therefore at high glucose levels when hexokinase activitiy is high
it is quickly inhibited by G-6-P. But glucokinase has a high Km
that is low affinity and is acts on Glucose only at high
concentrations and it is also not inhibited by G-6-P.
Question 40.
Allosteric enzymes are important for the regulation of metabolic
pathways. Allosteric enzymes have a different site other that its
substrate binding site where substances know as allosteric
effectors bind and control the enzyme action. Glucose-6- phosphate
is the allosteric inhibitor of hexokinase. AMP and ADP are the
allosteric activator of phosphofructokinase.
Question 46.
Option 4.
It is compared to confirm the sequence so that it only binds in
the 3' region of the gene of interest that we want to amplify by
PCR.
Question 48.
Option- 3
It is a passive transport through transmembrane integral
proteins. It doesn't requires any ATP hydrolysis as the ∆G for this
reaction is negative. And is driven by the concentration
gradient.
Question 47 cannot be done as the graph is not rendered with the
question.