1. Ignoring peptide length (or lack thereof) where would this portion of a polyp
ID: 3506553 • Letter: 1
Question
1. Ignoring peptide length (or lack thereof) where would this portion of a polypeptide be most likely to be found: On the inside or on the outside surface of a protein floating around in the cytoplasm? Tell me why.
2. A polypeptide chain has a large percentage of acidic and basic amino acids in it. The R groups of these amino acids form ionic interactions, which helps the protein to maintain it’s structure. This particular polypeptide works well under an optimum pH of 7. Ignoring effects of strong acids and bases on peptide bonds, what will happen to the tertiary structure of the protein if you move it stomach acid, which has a pH of 1-2. Why? Be specific regarding what influence the pH will have on the bonds maintaining tertiary structure in the molecule. Include the amino acid charges of the acidic and basic amino acids at the acidic pH, as well as the concept of pK in your answer. Assume that acidic amino acids have a pK of approximately 4.7 and basic amino acids have a pK of approximately 10.
3. Compare and contrast allosteric regulation, regulation by phosphorylation, and regulation by GTP/ATP.
4. Compare and contrast the catalytic mechanism of the serine protease (chymotrypsin) and lysozyme.
Explanation / Answer
ANSWER 1: Most of the aminoacids are synthesised with thehelp of two organelles of cell Endoplasmic reticulum (ER) and Ribosome. These polypeptide chains of amioacids found outside to the floating protein of cytoplasm and after formation the chain of polypeptide transported out to the external surface of cell membrane.
ANSWER 2 : The polypeptide chain of acidic and basic amino acids of tertiary structure when catalyse by the acidic pH of stomach (1-2) then its tertiary structure get deformed because it it maintained by placing of R group and other bond. But bonds did not affect by this due to these pK value.
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