Question

1. During muscle contraction, hydrolysis of ATP results in A) a change in the conformation of actin B) a change in the conformation of myosin C) association of myosin head to actin D) dissociation of myosin from actin E) no effect on muscle contraction 2. The steady state assumption, as a to monosubstrate enzyme kinetics, implies: A) Concentration of substrate is not changing B) Concentration of product is not changing C) Concentration of ES complex is not changing D) Formation rate of ES complex is not changing E) Formation rate of product is not changing 3. Trypsinogen is A) A gene coded for of trypsin B) An active enzyme C) the protease the catalyze the hydrolysis of trypsin D) Trypsin in its misfolded state E) The inactive precursor of trypsin 4. The allosteric effect of a regulator to an enzyme refers to A) binding of a regulator affects the binding the substrate B) binding of substrate affect the binding of protein to a regulator C) binding of regulator affect the catalytic property of the enzyme D) covalent binding of regulator affect the binding of substrate E) binding of regulator affect covalent catalytic property of enzyme 5. In hemoglobin, the transition from T state to R state (low to high affinity) triggered by: A) Fe2. binding to hemoglobin B) H binding to hemoglobin C 2 binding to hemoglobin D) H20 binding to hemoglobin E CO2 binding to hemoglobin 6. Carbon monoxide (CO) is toxic because: A) it binds to myoglobin and causes it to denature. B) it is rapidly converted to toxic Co2 1A.

Answer 1

Answer of the following Question

1 -Answer B- ATP binding to myosin lead to Change in conformation.

2-Answer-C -concentration of ES, not changing

3-Answer- C the catalyze the hydrolysis of trypsin.

4 Answer c- Binding of regulator affect the catalytic efficiency of the enzyme.

5-Answer c O₂ binding to hemoglobin.

6 Answer D. CO bind with Fe²⁺ and prevents the binding of O₂