Biochemistry Block 2 TopHat Questions

Concerning the structure of Hb, which is true?

o Hb not only has primary, secondary and tertiary structure, but includes quaternary
elements as well.
o Hb is a protein with a specific primary sequence of amino acids
o Hb binds both oxygen and carbon dioxide, which displace each other at the heme site
o Hb will bind oxygen most readily if the iron of heme is in the ferric oxidation state

Which is true concerning Hb and its ability to properly carry out is function in biochemistry?
o A tightly bound prosthetic group is a required component
o It requires a vitamin - iron - to be available in solution
o A cofactor - heme - must be at sufficient concentration
o The Apoprotein is required for full and complete function

Concerning the phenomenon of cooperativity, which of the following is correct?

o The direct cause is change in tertiary structure

o The ligand must interact with different types of sites
o It requires multiple binding sites on a protein
o It causes enhanced binding of a ligand

The binding of oxygen to hemoglobin is an example of which of the following?

o Heterotropic cooperativity
o Homotropic T to R strain
o Homotropic allosterism
o Heterotropic allosterism

Which of the following correctly describes the binding of CO2 to hemoglobin?

o Occurs on side chains of glutamate and aspartate residues

o It binds in a reversible reaction with free amine groups
o It displaces oxygen from the ferrous iron site of heme
o It occurs in the central core cavity of R state HB

Which of the following best describes the simplistic, bottom-line trend predicted by
thermodynamics?

o Lower entropy and higher enthalpy is favored

o The rate of a reaction is governed and regulated
o The trend is toward randomness and heat loss
 o The free energy of a specific reaction is constant
o n/a

In biochemistry, what is often the solution to the problem where a specific reaction is
required, but that reaction is not thermodynamically favored?

o Increased concentrations of reactants

o Utilize compartmentation to alter conditions
o Raise the ambient temperature
o Couple the reaction to another reaction

What important point was illustrated in our discussion of the reaction that adds an additional
nucleotide to a growing nucleic acid chain?

o The life span of high energy molecules can be long

o The triphosphate nucleotide remains in the chain
o A molecule of water is added to the nucleotide bond
o Destruction of a product makes the reaction irreversible

An enzyme catalyst facilitates passage of the substrate through a _____, in order to reach the
product.

o Conformational analogue
o Transition state
o Activation state
o Equilibrium state

A given amount of enzyme has a finite rate of product formation that can be achieved as the
concentration of substrate is increased. What is this value called

o Hyperbolic rate
o Terminal velocity
o Vmax
o Km

The special area within the three-dimensional area of an enzyme where the actual conversion
of substrate to product occurs is referred to as the?

o Transition site
o Allosteric site
o Active site
o Cofactor site
 How would you best describe the relationship between the affinity of a substrate for an
enzyme versus the value of Km?
o Directly proportional
o Related by the rate observed at Vmax
o Double-reciprocally related
o Inverse

Under what conditions is Km often considered to be essentially the same as Kd?

o When measuring initial velocity
o When product formation is great
o If K2 may be disregarded as negligible
o If allosterism has been considered by M-M

What is accomplished by the calculation of Kcat (Turnover Number)?

o A saturating amount of substrate is normalized
o If allosterism is present, Km is corrected
o Vmax is adjusted for the amount of enzyme
o Varying affinity of substrate is normalized