Allosteric Effects The conformational changes from the T to the R state is initiated by movement of the F-helix, which contains the proximal His reorganization of protein-protein contacts between the individual subunits binding of oxygen to the heme movement of the proximal histidine towards the heme movement of the F-helix, which contains the proximal His reorganization of protein-protein contacts between the individual subunits binding of oxygen to the heme movement of the proximal histidine towards the heme ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The Hill coefficient (nH) for myoglobin and hemoglobin are respectively 1.0 and 2.8 1.2 and 4.5 2.8 and 1.0 4.5 and 1.2 1.0 and 2.8 1.2 and 4.5 2.8 and 1.0 4.5 and 1.2 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The specificity of a ligand binding site on a protein is based on the absence of competing ligands the opposite chirality of the binding ligand the presence of hydrating water molecules the amino acid residues lining the binding site the absence of competing ligands the opposite chirality of the binding ligand the presence of hydrating water molecules the amino acid residues lining the binding site ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Small molecules affect hemoglobin (Hb) by increasing [H+] increasing [H+] and decreasing Hb affinity for O2 decreasing Hb affinity for O2 increasing Hb affinity for O2 increasing [H+] increasing [H+] and decreasing Hb affinity for O2 decreasing Hb affinity for O2 increasing Hb affinity for O2 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Bisphosphoglycerate (BPG) cannot bind to the oxygenated R state of hemoglobin because it is displaced from the heme by movement of the proximal histidine BPG binds to the R state with the same affinity as the T state its binding pocket becomes too small to accommodate BPG it is displaced from the heme by oxygen it is displaced from the heme by movement of the proximal histidine BPG binds to the R state with the same affinity as the T state its binding pocket becomes too small to accommodate BPG it is displaced from the heme by oxygen ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator stabilizes the R state of the protein both (a) and (c) increases the binding affinity decreases the binding affinity stabilizes the R state of the protein both (a) and (c) increases the binding affinity decreases the binding affinity ANSWER DOWNLOAD EXAMIANS APP
EXAMIANS