Type of bonds that stabilize a tertiary structure
of a protein include all the following except:
1. van der Waal’s interactions
2. Hydrophobic interactions
3. Disulfide linkage
4. Covalent bonds

Protein molecules that assist in the proper
folding of other proteins are known as:
1. Ubiquitins
2. Chaperonins
3. Prions
4. Calmodulins

A ribosome inhibiting secondary metabolite
protein found in the castor plant is:
1. Ricin

2. Abrin

3. Concanvalin A

4. Vinblastin

When an enzyme-substrate reaction tends
toward zero order, the only way to make a
reaction speed up is to:
1. Add more substrate
2. Add more enzyme
3. Increase the temperature
4. Increase the pressure in the medium

The Glucose transpoter protein present in the
baso-lateral surface of the intestinal epithelial
cells is:
1. GLUT 1

2. GLUT 2

3. GLUT 3

4. GLUT 4

The plot represents the relationship between
substrate concentration and velocity for a
single enzyme in the absence (curve x) and
presence (curve y) of a compound that binds
allosterically to the enzyme. The allosteric
compound is:

1. a competitive inhibitor.
2. a noncompetitive inhibitor.
3. an irreversible inhibitor.
4. an activator.

The metal ion that acts as a co-factor for both alcohol dehydrogenase and carbonic anhydrase is:

The living state can be best described as a:
1. non equilibrium steady state
2. non equilibrium non steady state
3. equilibrium non steady state
4. equilibrium steady state

The blood concentration of glucose in a normal healthy individual is:

All the following assumptions apply to Michaelis-Menten kinetic analyses of enzyme action EXCEPT:
1. the total enzyme concentration studied at each substrate concentration is fixed in analysis of enzyme kinetics.
2. formation of enzyme-substrate complex does not appreciably decrease the concentration of substrate.
3. Km decreases with competitive inhibition.
4. maximal velocity is reached when the enzyme-substrate complex is equal to the total concentration of enzyme present.