Protein Engineering vol. 9 no. 3 pp. 265-271, 1996
© 1996 Oxford University Press
RESEARCH-ARTICLE |
Analysis of protein conformational characteristics related to thermostability
1Institut de Biologia Fonamental and Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona Bellaterra, E-08193 Barcelona 2Departament de Ciències Mèdiques Bàsiques, Facultat de Medicina, Universitat de Lleida E-25198 Lleida, Spain
3To whom correspondence should be addressed
The thermal stability of proteins was studied, 195 single amino acid residue replacements reported elsewhere being analysed for several protein conformational characteristics: type of residue replacement; conservative versus nonconservative substitution; replacement being in a homologous stretch of amino acid residues; change in hydrogen bond, van der Waals and secondary structure propensities; solvent-accessible versus inaccessible replacement; type of secondary structure involved in the substitution; the physico-chemical characteristics to which the thermostability enhancement can be attributed; and the relationship of the replacement site to the folding intermediates of the protein, when known. From the above analyses, some general rules arise which suggest where amino acid substitutions can be made to enhance protein thermostability: substitutions are conservative according to the Dayhoff matrix; mainly occur on conserved stretches of residues; preferentially occur on solvent-accessible residues; maintain or enhance the secondary structure propensity upon substitution; contribute to neutralize the dipole moment of the caps of helices and strands; and tend to increase the number of potential hydrogen bonding or van der Waals contacts or improve hydrophobic packing.
Keywords: biotechnology/protein/protein engineering/proteinstructure/protein thermostability
Received June 15, 1995; revised November 1, 1995; accepted December 22, 1995.
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