Questions 2 and 3 Did your casein buffer seem to be more effective at moderating

Question

Questions 2 and 3 Did your casein buffer seem to be more effective at moderating the pH of strong acids or moderating the pH of strong bases? Please explain your answer. 1. Suppose a protein contains a large number of serine residues. Also suppose there is a mutant protein in which many of the serine residues have been replaced by valine residues. Do you think the mutant protein will be more hydrophilic than the normal protein, or more hydrophobic than the normal protein? 2. H :O: H :O: serine valine 3. Please explain your answer to the previous question. esidur of thr aming acid lysine in its uncharged form. Draw the structures of the

Explanation / Answer

The mutant will be more hydrophobic than normal protein this is because polar group present in the side chain of serine (i.e -CH2OH) has been replaced by hydrophobic group in valine.

The polar group in serine participates in hydrogen bonds as donors or acceptors thereby making it hydrphilic whereas in case of valine residue the side chain remains inside protein core making it more hydrophobic .

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