(1) A tertiary protein structure is held together in one region through an inter
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Question
(1) A tertiary protein structure is held together in one region through an interaction between two cysteine residues.What type of interaction is this?
(2) A mutant form of the protein develops that has arginine in place of one of the cysteine and aspartic acid in place of the other cysteine. Explain how this double mutant protein is able to maintain a bond in this region?
(3) Even though the mutant protein appears to be folded correctly, it is not able to function and/or be regulated correctly.Give 2 reasons why this is possible.(6 pts)
Explanation / Answer
1) The overall three dimensional arrangement of protein is called tertiary protein structure. The backbone of the tertiary structure is a single polypeptide chain & it also includes one or more protein domains. The structure is stabilized by disulfide bonds, hydrogen bonds between different side chains & also by the salt bridges & ionic interaction between positive & negative charged sites of amino acids. Among these disulfide bond between two cysteine groups is one of the important interaction for stabilization of tertiary structure.
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