The pKA of histidine in a protein active site where it is next to an aspartate or glutamate would be____________ the pKa of free histidine solution
higher, lower, no different
Is it higher??© BrainMass Inc. brainmass.com October 24, 2018, 9:57 pm ad1c9bdddf
To answer this question, we need to know what pKa means.
pKa = -log Ka
So, what does that tell us? What is Ka? That is the dissociation or ionization constant for an acid.
HA + H2O <------> A- + H3O+
Ka = [A-][H3O+]/[HA]
Therefore, the more that the acid dissociates in water, the larger the Ka. The Ka is a measure of the degree of ionization of an acid in water. A ...
The expert examines Pka histidine protein active site.
Respiratory Physiology, Myoglobin & Hemoglobin Structure
Hemoglobin & Transport of O2 & CO2
Include drawings, equations, graphs, etc. where appropriate.
1. Define the following: prosthetic group, fractional saturation, allosterism, cooperativity, Bohr effect, isohydric carriage, respiratory acidosis & alkalosis, metabolic acidosis & alkalosis. Please provide examples.
2. Describe the interactions (e.g., H-bonding) that are involved in the tight binding of heme to apomyoglobin?
3. Describe Myoglobin's structure (include comments on its primary, secondary, tertiary and quaternary structure).
4. What are the major similarities and differences in structure and properties between myoglobin and hemoglobin? Provide descriptions.
5. What are the structural & functional aspects of the effect of H+ on the O2 binding of hemoglobin? Include any pKa differences, at least one example of a specific functional group involved, etc. What are the consequences of this binding? How does it effect the body in the lungs and in the periphery?View Full Posting Details