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The influence of molecular variation on protein interactions
Author(s) -
Ho Jason G. S.,
Middelberg Anton P. J.
Publication year - 2003
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.10815
Subject(s) - solvation , lysozyme , egg white , chemistry , surface protein , implicit solvation , accessible surface area , chemical physics , computational chemistry , molecule , biochemistry , biology , organic chemistry , virology
We investigated the influence of solvation forces on protein–protein interactions for two forms of lysozyme: hen egg white (HEWL) and turkey egg white (TEWL). Turkey egg white has more surface exposed hydrophobic residues than HEWL and the protein–protein interactions of TEWL are shown to be more attractive than those of HEWL, for the conditions studied. The importance of including a solvation term in the potential of mean force model, to account for molecular variation in protein surface characteristics, is highlighted. We also show that the magnitude of this solvation term can be estimated using readily available data. © 2003 Wiley Periodicals, Inc. Biotechnol Bioeng 84: 611–616, 2003.