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How Nature Engineers Protein (Thermo) Stability

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Life Under Extreme Conditions

Abstract

It is generally accepted that the amino acid sequence of a protein determines its unique three-dimensional structure, which in turn dictates the protein biological function (Anfinsen 1973; Anfinsen and Scheraga 1975). At the present, the structures of some 400 globular proteins have been solved by X-ray crystallography; this wealth of structural information has illustrated the subtle ways in which amino acid chains fold into stable globular structures (Richardson 1981). One of the key problems in modern biochemistry and biophysics is to understand the physical principles and forces, as well as mechanistic pathways, leading to folded proteins. This problem is presently the subject of intense research by a great number of investigators using a variety of theoretical and experimental techniques (Creighton 1978, 1985, 1988; Ghélis and Yon 1982; Jaenicke 1987). However, a quantitative understanding is still lacking of the roles of individual amino acid residues in both directing protein folding and stabilizing protein structure. Only the solution of the protein folding and stability problem will pave the way to prediction of the three-dimensional structure of a protein merely on the basis of its known amino acid sequence, as well as to the design of new proteins with desired biological and physicochemical properties (de novo protein design; Salemme 1985; Oxender and Fox 1987; Ohlendorf et al. 1987; De Grado 1988; Goldenberg 1988).

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  1. Department of Organic Chemistry, Biopolymer Research, Centre of CNR, University of Padua, Padua, Italy

    A. Fontana

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  1. Institute of Protein Biochemistry and Enzymology (IBPE), Italian National Research Council, Via Marconi 10, I-80125, Naples, Italy

    Guido di Prisco

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Fontana, A. (1991). How Nature Engineers Protein (Thermo) Stability. In: di Prisco, G. (eds) Life Under Extreme Conditions. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-76056-3_6

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