ISSN:
0887-3585
Keywords:
hydration
;
PMF
;
solvent-induced forces
;
molecular dynamics
;
BPTI
;
protein folding
;
funneling and recognition
;
energy landscapes
;
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Medicine
Notes:
Molecular dynamics simulations of model solutes in explicit molecular water have recently elicited novel aspects of the strong nonpair additivity of the potential of mean force (PMF) and related solvent-induced forces (SIFs) and hydration. Here we present the results of the same type of work on SIFs acting on bovine pancreatic trypsin inhibitor (BPTI) at single residue/sidechain resolution. In this system, nonpair additivity and the consequent dependence of SIFs on the protein conformational context are sufficiently strong to overturn SIFs on some individual residues, relative to expectations based on their individual characters. This finding calls for a revisitation and offers a richer and diversified understanding of the role of hydrophobic/philic/charged groups in establishing the exquisite specificity of biomolecular folding and functional conformation. Its relevance is appreciated by noting that the work of a typical SIF acting on one residue, when displaced across a distance of 1 Å, is the equivalent of up to a few kcal/mol, which is the range of the stability/function free energy of a protein. Proteins 32:129-135, 1998. © 1998 Wiley-Liss, Inc.
Additional Material:
3 Ill.
Type of Medium:
Electronic Resource
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