To charge or not to charge?
The ability to engineer proteins with increased thermostability will profoundly broaden their practical applications. Recent experimental results show that optimization of charge-charge interactions on the surface of proteins can be a useful strategy in the design of thermostable enzymes. Results also indicate a possibility that such optimized interactions provide structural determinants for enhanced stability of proteins from thermophilic organisms. In this article, the general strategy for design of thermostable proteins and perspectives for future studies are discussed.
Faculty of Science, Department of Chemical Physics and Institute of Biotechnology, University of Granada, 18071-Granada, Spain. sanchezr@goliat.ugr.es
J M
JM
Sanchez-Ruiz
G I
GI
Makhatadze
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000737:chemistry; D006360:Heat-Shock Proteins; D008969:Molecular Sequence Data; D009154:Mutation; D011489:Protein Denaturation; D015202:Protein Engineering / Q000379:methods*; D011506:Proteins / Q000737:chemistry* / Q000235:genetics; D055672:Static Electricity; D013816:Thermodynamics
D001426:Bacterial Proteins; D002352:Carrier Proteins; D006360:Heat-Shock Proteins; D011506:Proteins; C077188:cold-shock protein CspB, Bacteria