Authors: Renugopalakrishnan, V.; Garduño-Juárez, R.; Narasimhan, G.; Verma, C.S.; Wei, X.; Li, Pingzuo

Source: Journal of Nanoscience and Nanotechnology, Volume 5, Number 11, November 2005 , pp. 1759-1767(9)

Publisher: American Scientific Publishers

Abstract:

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 proteins remain physiologically active and are available for technological applications (answers may emerge from the discovery of new, natural hyperthermophilic enzymes that are active above 125 °C or from the selection of mutants of hyperthermophilic enzymes that are more stable); second, the use of hyperthermophilic enzymes as molecular templates to design highly stable enzymes that have high activity at low temperatures; third, the link between rigidity and flexibility to thermostability and activity, respectively. We review progress in these areas.

Keywords: THERMALLY STABLE PROTEIN; RATIONAL DESIGN; PROTEIN THERMAL STABILITY; BACTERIORHODOPSIN; RUBREDOXIN; FERREDOXIN

Document Type: Review article

DOI: http://dx.doi.org/10.1166/jnn.2005.441

Publication date: 2005-11-01

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