What forces contribute to the folding of a polypeptide? Can you explain the reasoning too?

The hemoglobin in the fetus (HbF) is a structural variant of the hemoglobin in the mother (HbA). HbA is a tetrameric protein complex consisting of two α-globin and two β-globin subunits. HbF is made up of two αglobin and two γ-globin subunits, where the γ-globins are similar to the β-globins but γglobins have lower affinity for 2,3- bisphosphoglycerate or BPG. Studies of oxygen transport in pregnant mammals show that the oxygen-saturation curves between the red blood cells of the fetus and the mother are markedly different. 1. The shape of hemoglobin binding curves is: hyperbolic or sigmoidal 2. a) Based on the binding curves, determine the dissociation constant (Kd) for each hemoglobin complex. (Show correct units.) Kd of HbF + BPG: ________________ Kd of HbA + BPG: _____________________ b) Which has a higher affinity for oxygen? HbF+BPG HbA+BPG 3. a) How many BPG molecule(s) is/are expected to bind one hemoglobin complex? 1 2 3 4 b) BPG binding preferentially stabilizes which state…

Disulfide linkages are uncommon in cytoplasmic proteins, whereas they are common in extracellular proteins. Why?

Certain enzymes catalyze the covalent linkage of an acetyl group to lysine amino acids as shown below. When a particular target protein is in the un-acetylated state, its interacting partner protein will not bind. However, once acetylated, the partner protein can bind to this target protein. Which of the following can you conclude? Select all that apply CH CO NH 3. NH Lysine acetylation reaction CH, CH, +HaN -C- CO- H. HIN-C- Co- H. UAcetylation changes the secondary structure of the target protein The partner protein has acidic residues in the interacting region Acetylation changes the tertiary structure of the target protein The partner protein has basic residues in the interacting region 8-1-8-8-8–8–d=