Other Case

Herning performed a detailed DSC study of several mutants of human lysozyme involving proline and glycine residues. Val110Pro and Ala47Pro mutants has made the protein slightly stable. But in case of Pro/Gly mutation, the situation is more difficult. A Pro71Gly replacement led to a distinct destabilization, which caused by entropic origin. By contrast, the mutant Pro103/Gly led to apparent effect on protein stability.

Mainfroid has made mutations on human triosephosphate isomerase dimer. They found that Ala->Pro mutation has contributed up to 0.6 kcal/mol to stabilty by reducing the entropy of the unfolded protein

Thermodynamic Parameters of Human lysozyme mutants studied.