BIOCHEMISTRY: Protein stability and denaturation A study looked at mutations in

Question

BIOCHEMISTRY: Protein stability and denaturation

A study looked at mutations in the hydrophobic core of a protein of interest. The Tm for the wild-type protein (no mutations) was compared with that of a few site-directed mutants. The data is shown below:

Wild-type 53.5 oC

L46A          43 oC

L118A       40 oC

L99A         36 oC

Why do all of these mutants substitute alanine for the naturally-occurring amino acid? Is this a good substitution?

BIOCHEMISTRY: Protein stability and denaturation A study looked at mutations in the hydrophobic core of a protein of interest. The Tm for the wild-type protein (no mutations) was compared with that of a few site-directed mutants. The data is shown below: Wild-type 53.5 degree C L46A 43 degree C L118A 40 degree C L99A 36 degree C Why do all of these mutants substitute alanine for the naturally-occurring amino acid? Is this a good substitution?

Explanation / Answer

frameshift mutations are substituting Alanine instead of leucine.

however, since these mutations are lowering the Tm for the protein, i.e. lowering G-C content of the aminoacid peptide chain, thus, these mutations are not good. as they are making protein structure less thermostable. causing it to denature at lower temp.

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