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Protein stability and electrostatic interactions between solvent exposed charged side chains
Author(s) -
Akke Mikael,
Forsén Sture
Publication year - 1990
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340080106
Subject(s) - side chain , chemistry , electrostatics , static electricity , globular protein , crystallography , mutant , solvent , wild type , accessible surface area , computational chemistry , biochemistry , organic chemistry , physics , quantum mechanics , gene , polymer
To investigate the contribution to protein stability of electrostatic interactions between charged surface residues, we have studied the effect of substituting three negatively charged solvent exposed residues with their side‐chain amide analogs in bovine calbindin D 9k —a small (M r 8,500) globular protein of the calmodulin superfamily. The free energy of urea‐induced unfolding for the wildtype and seven mutant proteins has been measured. The mutant proteins have increased stability towards unfolding relative to the wildtype. The experimental results correlate reasonably well with theoretically calculated relative free energies of unfolding and show that electrostatic interactions between charges on the surface of a protein can have significant effects on protein stability.