Hydrophobic-hydrophilic forces in protein folding.

Abstract:

: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.

journal_name

Biopolymers

journal_title

Biopolymers

authors

Durell SR,Ben-Naim A

doi

10.1002/bip.23020

subject

Has Abstract

pub_date

2017-08-01 00:00:00

issue

8

eissn

0006-3525

issn

1097-0282

journal_volume

107

pub_type

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