Approximate P50 for myoglobin from its binding curve. Approximate P50 for normal hemoglobin and the hemoglobin mutant from the binding curve. At low pO2 (below 20 Torr), which binds O2 with greater affinity, normal hemoglobin or the hemoglobin mutant?

From the Hill Plot below, the of the first binding event for the receptor-ligand system under study is: Q1 4nM Ο 10 μΜ -2 nM 2 nM Calculate the Hill Coefficient from the receptor-ligand binding data below: Q2 4 100 2 3 (0-1) 60 log 10 8 6 4 2 0 -2 -4 -6 -6 -4 -2 0 2 4 log [L] (nM) 6 8 10

Draw a diagram of the "general model" aka “protein-protein interaction model" of suppression to show how it works (or how it can be used to find interacting proteins.)

. What physiological effect would you predict from a mutation that replaced with serine the cysteine in the constant part of the immunoglobulin light chain that is involved in disulfide-bond for- mation with the heavy chain? ,

The binding of 2,3-bisphosphoglycerate is lowest with: OA) Adult hemoglobin OB) Fetal hemoglobin OC) Sickle cell hemoglobin OD) It is the same for all three

The 2-3 phosphoglycerate (BFG) binds to the central gap formed by the hemoglobin monomers (a2b2) facilitating the reversible release of oxygen. Approximate relationships between BFG concentrations in red blood cells and Pos in hemoglobin are in the table.a) Draw the reaction schemeb) Write the forces that condition the union between hemoglobin and BFG

Why does release of BPG in the blood system help counter the effects of high altitude induced hypoxia? O BPG binds each hemoglobin tetramer and leads to formation of a confirmation that binds 02 more strongly allowing uptake of 02 in the lungs BPG binds myoglobin and leads to formation of a confirmation that binds 02 more strongly allowing uptake of O2 in the lungs BPG binds myoglobin and leads to formation of a confirmation that binds 02 more weakly allowing release of 02 in oxygen starved tissues O BPG binds each hemoglobin tetramer and leads to formation of a confirmation that binds 02 more weakly allowing release of 02 in oxygen starved tissues

Briefly explain the Warburg Effect. How can the Warburg effect be taken advantage of (HINT: make sure to give DETAILS on the pathway, and molecules / mechanism involved)?

Given the following, calculate Gk: ENa = +45 mV; Ek = -85 mV; ECl = -60 mV; GNa = 5x10-8 S; GCl =0; Vm = -70 mV

Normal Hgb is referred to as HbA and contains 4 subunits, 2 a-globin chains and 2 B-globin chains, arranged as two dimers of aß. In Sickle Cell Disease, both B-globin chains are altered in the dimers (aßS/aßS). Q3: Which level of structure does the aß/aß and aßS/aßS in HbA and HbS describe?