BIOCHEMISTRY: Protein stability and denaturation A study looked at mutations in
ID: 38469 • Letter: B
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.