Kramer's equation suggests the dramatic increase in this quantity observed in thermophilic enzymes operating below their temperature breakpoint can be explained by a change in protein flexibility.
Kramer's equation suggests the dramatic increase in this quantity observed in thermophilic enzymes operating below their temperature breakpoint can be explained by a change in protein flexibility. Collision theory fails to accurately predict this quantity in situations involving "loose", high-entropy transition states, where this quantity tends to be large. It can be used to calculate the steric factor because this quantity is the fraction of total collisions between molecules that occur with the proper orientation for the reaction to proceed. It is defined as the product of the Boltzmann constant and temperature divided by Planck's constant in the Eyring equation. This quantity can be determined graphically by finding the y-intercept of the graph of the natural log of a reaction's rate constant against inverse temperature. This factor gives the dependency of the rate constant K upon temperature and activation energy. For 10 points, name this component of the Arrhenius equation that is symbolized A.
Kramer's equation suggests the dramatic increase in this quantity observed in thermophilic enzymes operating below their temperature breakpoint can be explained by a change in protein flexibility.
pre-exponential factor [or frequency factor; accept A before it is mentioned and prompt on it afterwards; prompt on Z; prompt on "steric factor" before "Boltzmann constant" is read; prompt on "collision factor"]