par Gilis, Dimitri 
;Wintjens, René ;Rooman, Marianne
Editeur scientifique Pandalai, S. G.
Référence Recent research developments in protein engineering, Research Signpost, Trivandrum, India, Vol. 1, Ed. 1, page (277-290)
Publication Publié, 2001
;Wintjens, René ;Rooman, Marianne Editeur scientifique Pandalai, S. G.
Référence Recent research developments in protein engineering, Research Signpost, Trivandrum, India, Vol. 1, Ed. 1, page (277-290)
Publication Publié, 2001
Partie d'ouvrage collectif
| Résumé : | Several types of computer-aided methods have been developed for evaluating thermodynamic stability changes of proteins caused by mutations. Some use detailed atomic description and force fields and are too computer-time consuming to be applied to more than a few mutations, whereas others use residue-based descriptions and database-derived potentials and are designed to predict rapidly the stability changes of large sets of mutations in a given protein and to select the most (de)stabilizing ones, and may be of great help in rational design of modified proteins. Thermal stability changes upon mutation may be estimated from thermodynamic stability changes under the assumption that the change in melting temperature is proportional to the change in folding free energy, which is often verified. They can also be evaluated directly, but up to now only a few qualitative rules have been found, among whioch the higher frequency of surface salt bridges in thermophilic than in mesophilic proteins. |
