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Protein Engineering, Vol. 16, No. 4, 279-286, April 2003
© 2003 Oxford University Press

A simple electrostatic criterion for predicting the thermal stability of proteins

Angel Mozo-Villarías1,2, Juan Cedano3 and Enrique Querol3

1 Departament de Ciències Mèdiques Bàsiques, Facultat de Medicina, Universitat de Lleida, Avda. Rovira Roure 44, 25198 Lleida and 3 Institut de Biotecnologia i Biomedicina, Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, Bellaterra, Barcelona, Spain

2 To whom correspondence should be addressed. E-mail: angel.mozo{at}cmb.udl.es

The enhancement of protein thermostability is an important issue for both basic science and biotechnology purposes. We have developed a thermostability criterion for a protein in terms of a quasi-electric dipole moment (contributed by its charged residues) defined for an electric charge distribution whose total charge is not zero. It was found that minimization of the modulus of this dipole moment increased its thermal stability, as demonstrated by surveying these values in pairs of mesostable–thermostable homologous proteins and in mutations described in the literature. The analysis of these observations provides criteria for thermostabilization of a protein, by computing its dipole profile. This profile is obtained by direct substitution of each amino acid of the sequence by either a positive, negative or neutral amino acid, followed by a recalculation of the dipole moment. As an experimental example, these criteria were applied to a ß-glucanase to enhance its thermal stability.


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