A tertiary protein structure is held together in one region through an interacti

Question

A tertiary protein structure is held together in one region through an interaction between two cysteine residues. What type of interaction is this? 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? 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.

Explanation / Answer

1. Disulfide bond
Cys has sulphur containing amino acid.
Two cys join together by disulphide bond.

2. Arg - Postive charge amino acids
Asp - Negative charged amino acids

Charged amino acid side chains can form ionic bonds.

Ionic bond totally different from disulphide bond so conformation of protein is slightly different.

Disilfide bond more strong than ionic bond.

Related Questions

Navigate

• Browse (All)
• Browse A
• Subjects

Integrity-first tutoring: explanations and feedback only — we do not complete graded work. Learn more.