A non-competitive inhibitor of an enzyme catalyzed reaction
1. binds to the Michaelis complex (ES).
2. increases Vmax.
3. is without effect at saturating substrate concentrations.
4. can actually increase reaction velocity in rare cases.

The measurement of which of the following would be indicator of the degree of inhibition by a competitive enzyme inhibitor?
1. V_max
2. The y-intercept on a Limeweaver-Burke Plot
3. Km
4. ¼ V_max

An allosteric inhibitor of an enzyme usually
1. binds to the active site.
2. participates in feedback regulation.
3. denatures the enzyme.
4. causes the enzyme to work faster.

A change in an amino acid located distantly from the active site of an enzyme can affect the specificity of the enzyme towards its substrate by:

The property of water that enables it to
stabilize temperature in bodies of organisms
and thus makes it indispensible for life is:
1. High specific heat
2. High latent heat of fusion
3. High latent heat of vaporization
4. High cohesion and adhesion

The element that makes up the highest
percent weight of the human body is:
1. Carbon
2. Hydrogen
3. Oxygen
4. Nitrogen

The number of high energy bonds in a molecule of ATP is:

The molecule that is never branched and is
straight is:
1. Amylose
2. Amylopectin
3. Glycogen
4. Cellulose

An amino acid that is negative charged amongst the following will be:

The correct ascending order of percent composition of various components of a typical cell would be:
1. Protein – Carbohydrate – Lipids – Nucleic acids
2. Protein – Nucleic acids – Carbohydrate – Lipids
3. Carbohydrates – Protein – Nucleic acids– Lipids
4. Carbohydrates – Protein – Lipids – Nucleic acids