The amino acid sequence of a protein affects both its structure and its function. Thus, the
ability to modify the sequence, and hence the structure and activity, of individual proteins in …

During the past 15 years there has been a continuous flow of reports describing proteins
stabilized by the introduction of mutations. These reports span a period from pioneering …

Flexible sites are potential targets for engineering the stability of enzymes. Nevertheless, the
success rate of the rigidifying flexible sites (RFS) strategy is still low due to a limited …

Modern enzyme development relies to an increasing extent on strategies based on diversity
generation followed by screening for variants with optimised properties. In principle, these …

Organismal adaptation to extreme temperatures yields enzymes with distinct configurational
stabilities, including thermophilic and psychrophilic enzymes, which are adapted to high and …

The pervasive influence of temperature on biological systems necessitates a suite of
temperature—compensatory adaptations that span all levels of biological organization …

From a chemical point of view, enzymes are by far the most structurally complex and
functionally sophisticated molecules known. This is perhaps not surprising, once one …

The use of enzymes for industrial and biomedical applications is limited to their function at
elevated temperatures. The principles of thermostability engineering need to be …

Systematic approaches to directed evolution of proteins have been documented since the
1970s. The ability to recruit new protein functions arises from the considerable substrate …

Recent experiments suggested that ATP can effectively stabilize protein structure and inhibit
protein aggregation when its concentration is less than 10 mM, which is significantly lower …