Home⇒ Medical Science⇒ Biochemistry⇒ Allosteric effects
| 1-Dont try to cram or spend more time here just read it fast and cover syllabus then practice MCQ's cheptor of same topic to check your progress. . |
| 2-Wrong options are also given but dont concentrate there, Right answer is in bold format. |
| Q1 ⇒ The Hill coefficient (nH) for myoglobin and hemoglobin are respectively 1.0 and 2.8 [other wrong options] [Discuss in forum] |
| Q2 ⇒ Small molecules affect hemoglobin (Hb) by increasing [H+] and decreasing Hb affinity for O2 [other wrong options] [Discuss in forum] |
| Q3 ⇒ The conformational changes from the T to the R state is initiated by binding of oxygen to the heme [other wrong options] [Discuss in forum] |
| Q4 ⇒ In hemoglobin, allosteric effects occur to maximize oxygen delivery to the tissues [other wrong options] [Discuss in forum] |
| Q5 ⇒ An allosteric activator both (a) and (c) [other wrong options] [Discuss in forum] |
| Q6 ⇒ The specificity of a ligand binding site on a protein is based on the amino acid residues lining the binding site [other wrong options] [Discuss in forum] |
| Q7 ⇒ O2 binding to hemoglobin results in both (a) and (b) [other wrong options] [Discuss in forum] |
| Q8 ⇒ A protein that shows infinite cooperative for binding of n ligands will both (b) and (c) [other wrong options] [Discuss in forum] |
| Q9 ⇒ A protein that binds two ligands in a non-cooperative manner will show both (b) and (c) [other wrong options] [Discuss in forum] |
| Q10 ⇒ When protein binds two ligands in a non-cooperative manner, then the x-intercept of the Scatchard Plot is 2 [other wrong options] [Discuss in forum] |
| Q11 ⇒ Bisphosphoglycerate (BPG) cannot bind to the oxygenated R state of hemoglobin because its binding pocket becomes too small to accommodate BPG [other wrong options] [Discuss in forum] |