Recent large-scale studies illustrate the importance of electrostatic interactions near the
surface of proteins as a major factor in enhancing thermal stability. Mutagenesis studies …

In general, enzyme thermostability is an intrinsic property, determined by the primary
structure of the protein. However, external environmental factors including cations …

Publisher Summary This chapter describes a promising strategy for obtaining new stable
enzymes—that is, to isolate them from micro-organisms that grow under extreme conditions …

The ability to engineer proteins with increased thermostability will profoundly broaden their
practical applications. Recent experimental results show that optimization of charge–charge …

Design of thermally stable proteins is spurred by their applications in bionanotechnology.
There are three major issues governing this: first, the upper limit on the temperature at which …

Publisher Summary This chapter outlines the evolutionary protein design methods that are
used to help uncover the molecular basis for temperature adaptation in enzymes. The …

Some enzymes, such as those from extreme thermophiles, have significant half-lives above
100° C. The differences in structure and function between these very stable and less stable …

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 boiled enzyme was toppled as a standard enzymology control when researchers in the
1970s started uncovering enzymes that loved the heat (1). Identification of a variety of …

Current theories agree that there appears to be no unique feature responsible for the
remarkable heat stability properties of hyperthermostable proteins. A concerted action of …