Enzymes synthesized by hyperthermophiles (bacteria and archaea with optimal growth
temperatures of> 80° C), also called hyperthermophilic enzymes, are typically thermostable …

It is now clear that the understanding of halophilic adaptation at a molecular level requires a
strategy of complementary experiments, combining molecular biology, biochemistry, and …

Modeling the effect of sequence variation on function is a fundamental problem for
understanding and designing proteins. Since evolution encodes information about function …

Researchers in both academia and industry have expressed strong interest in
comprehending the mechanisms responsible for enhancing the thermostability of proteins …

Three complete genome sequences of thermophilic bacteria provide a wealth of information
challenging current ideas concerning phylogeny and evolution, as well as the determinants …

Referee: Dr. Ruth Nussinov, Saic Frederick, Bldg. 469. 469, Room 151, Frederick, MD
21702-1201 Hyperthermophilic organisms optimally grow close to the boiling point of water …

The crystal structure of the closed form of citrate synthase, with citrate and CoA bound, from
the hyperthermophilic Archaeon Pyrococcus furiosus has been determined to 1.9 Å. This …

Thermally stable proteins are of interest for several reasons. They can be used to improve
the efficiency of many industrial processes and provide insight into the general mechanisms …

Salt bridges have been proposed to play a crucial role in promoting hyperthermostability in
proteins, yet they appear to make little contribution to protein stability at room temperature …

Electrostatic contributions to the folding free energy of several hyperthermophilic proteins
and their mesophilic homologs are calculated. In all the cases studied, electrostatic …