Solvent effect on binding thermodynamics of biopolymers.

Abstract:

:The indirect solvent-induced effect on the free energy of binding of biopolymers is examined within the framework of classical statistical mechanics. We focus specifically on the role of the solute-solvent hydrogen bonding. In particular, we have estimated the first order solvent effect on the indirect interaction between two biopolymers. We find that the solvent-induced interactions between two hydrophilic groups through water-bridged hydrogen bonds could significantly enhance the binding free energy. Some preliminary estimates indicate that this effect is significant and perhaps could be crucial in molecular recognition processes. Furthermore, we have calculated, from crystal structure data, the distance distribution between all the oxygens and nitrogens on the surface of some proteins that do not belong to the binding domain. In most cases we found an enhanced peak in the range of 4-5 A, which is where we expect to find strong solvent-induced interactions.

journal_name

Biopolymers

journal_title

Biopolymers

authors

Ben-Naim A,Ting KL,Jernigan RL

doi

10.1002/bip.360290604

subject

Has Abstract

pub_date

1990-05-01 00:00:00

pages

901-19

issue

6-7

eissn

0006-3525

issn

1097-0282

journal_volume

29

pub_type

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