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Hydrophobic‐hydrophilic forces in protein folding
Author(s) -
Durell Stewart R.,
BenNaim Arieh
Publication year - 2017
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.23020
Subject(s) - chemistry , hydrogen bond , hydrophobic effect , solvent , folding (dsp implementation) , protein folding , chemical physics , molecular dynamics , polar , molecule , computational chemistry , crystallography , organic chemistry , biochemistry , physics , astronomy , electrical engineering , engineering
The process of protein folding is obviously driven by forces exerted on the atoms of the amino‐acid chain. These forces arise from interactions with other parts of the protein itself ( direct forces), as well as from interactions with the solvent ( solvent‐induced forces ). We present a statistical–mechanical formalism that describes both these direct and indirect, solvent‐induced thermodynamic forces on groups of the protein. We focus on 2 kinds of protein groups, commonly referred to as hydrophobic and hydrophilic. Analysis of this result leads to the conclusion that the forces on hydrophilic groups are in general stronger than on hydrophobic groups. This is then tested and verified by a series of molecular dynamics simulations, examining both hydrophobic alkanes of different sizes and hydrophilic moieties represented by polar‐neutral hydroxyl groups. The magnitude of the force on assemblies of hydrophilic groups is dependent on their relative orientation: with 2 to 4 times larger forces on groups that are able to form one or more direct hydrogen bonds.