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Hydrophobic tendencies of polar groups as a major force in molecular recognition
Author(s) -
Chalikian Tigran V.
Publication year - 2003
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.10538
Subject(s) - chemistry , hydrogen bond , polar , steric effects , hydrophobic effect , nucleic acid , folding (dsp implementation) , solvent , macromolecule , crystallography , molecular recognition , chemical physics , molecule , stereochemistry , organic chemistry , biochemistry , physics , astronomy , electrical engineering , engineering
Proteins and nucleic acids are able to adopt their native conformation and perform their biological role only in the presence of water with which they actively interact in a mutually modifying way. Traditionally, hydrophobic effect has been considered to be the major factor stabilizing biopolymeric structures. However, solvent reorganization around polar groups is an event thermodynamically more unfavorable than solvent reorganization around nonpolar groups. Consequently, burial of polar groups with formation of complementary solute‐solute hydrogen bonds out of contact with water is an energetically favorable process that also provides a major force driving macromolecular association and folding. In contrast to nonpolar groups, polar groups may form their complementary intra‐ or intersolute hydrogen bonds out of contact with water only provided that an appropriate solute structure has been formed with properly positioned hydrogen bond donors and acceptors. Formation of such structures is disfavored entropically and may not be possible due to steric reasons. However, the interior of a folded protein, α‐helices and β‐sheets, double helical nucleic acid structures, and protein‐ligand interfaces all provide rigid matrices where polar groups may form their complementary hydrogen bonds. For these structures, the inward drive of polar groups represents a considerable stabilizing factor. © 2003 Wiley Periodicals, Inc. Biopolymers 70: 492–496, 2003