B. Why is Charybdotoxin a very stable protein? C. How might charybdotoxin\'s sta
ID: 188007 • Letter: B
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B. Why is Charybdotoxin a very stable protein? C. How might charybdotoxin's stability affect its ability to be a good toxin? 4. Predict what would happen to the function of the potassium channel if an amino acid in the center of the pore was replaced by a hydrophobic amino acid. B. Hemoglobin. 1. How many subunits make up the quaternary structure of hemoglobin? A. How many oxygen molecules can hemoglobin bind to at one time? B. Read "cooperation makes it easier" section on hemoglobin and explain why it is initially hard for the first oxygen to bind to hemoglobin.Explanation / Answer
B. Charybdotoxin Stability: This protein is very stable structure due to its compact, well-organized natural motif got more stability by three disulfide bonds in its basic scaffold. It has only 37 amino acids that also contribute to the stability of the structure for this protein. In its basic structure it is formed of short helix on one face and an antiparallel triple-stranded 1l-sheet on the opposite face.
C. The structure stability of this protein makes it a good toxin produced by scorpions as blocks homotetrameric, voltage-gated K+channels by binding near the outer membrane in one of the four indistinguishable orientations. The structure stability made it less sensitive towards enzymatic cleavage as well.
4. If one of the amino acid will be replaced by hydrophobic amino acid, then it will be unable to interact in the aqeous environment that will lead to the decrease in the effectivity of the protein to enter the plasms membrane. As hydrophobic amino acids are unable to form hydrogen bonding it will be causing the decrease in the effectivity of this protein to trigger its effect.
B. Quarternary structure of haemoglobin is composed of tetramer consisting of two dimmers include four polypeptide subunits; 2 alpha chains and two beta chains.
B. 1. A haemoglobin molecule can bind 4 oxygen molecules at a time. Because each polypeptide of haemoglobin has haem prosthetic group. One haem can bind to one oxygen, and hence four haem groups per haemoglobin molecule binds four oxygen molecules.
B. 2. Binding of oxygen to the haem group of haemoglobin is an allosterically regulated process, which means binding of one oxygen makes it easier to bind the next oxygen cooperatively. So the affinity constant of the first oxygen is lesser as compared to the rest. In this way it will take more energy to bind the first oxygen to the haemoglobin.
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