Entropy-enthalpy compensation of biomolecular systems in aqueous phase: A dry perspective

Liviu Movileanu; Eric A. Schiff

doi:10.1007/s00706-012-0839-9

Entropy-enthalpy compensation of biomolecular systems in aqueous phase: A dry perspective

Liviu Movileanu, Eric A. Schiff

Research output: Contribution to journal › Article › peer-review

17 Scopus citations

Abstract

We survey thermodynamic measurements on processes involving biological macromolecules in aqueous solution, which illustrate well the ubiquitous phenomenon of entropy-enthalpy compensation. The processes include protein folding/unfolding and ligand binding/unbinding, with compensation temperatures varying by about 50 K around an average near 293 K. We show that incorporating both near-exact entropy-enthalpy compensation (due to solvent relaxation) and multi-excitation entropy (from vibrational quanta) leads to a compensation temperature in water of about 230 K. We illustrate a general procedure for subtracting solvent and environment-related terms to determine the bare Gibbs free energy changes of chemical processes.

Original language	English (US)
Pages (from-to)	59-65
Number of pages	7
Journal	Monatshefte fur Chemie
Volume	144
Issue number	1
DOIs	https://doi.org/10.1007/s00706-012-0839-9
State	Published - Jan 2013

Keywords

Biological macromolecules
Entropy-enthalpy compensation
Hydrophobic interactions
Macromolecules

ASJC Scopus subject areas

General Chemistry

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10.1007/s00706-012-0839-9

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title = "Entropy-enthalpy compensation of biomolecular systems in aqueous phase: A dry perspective",

abstract = "We survey thermodynamic measurements on processes involving biological macromolecules in aqueous solution, which illustrate well the ubiquitous phenomenon of entropy-enthalpy compensation. The processes include protein folding/unfolding and ligand binding/unbinding, with compensation temperatures varying by about 50 K around an average near 293 K. We show that incorporating both near-exact entropy-enthalpy compensation (due to solvent relaxation) and multi-excitation entropy (from vibrational quanta) leads to a compensation temperature in water of about 230 K. We illustrate a general procedure for subtracting solvent and environment-related terms to determine the bare Gibbs free energy changes of chemical processes.",

keywords = "Biological macromolecules, Entropy-enthalpy compensation, Hydrophobic interactions, Macromolecules",

author = "Liviu Movileanu and Schiff, {Eric A.}",

note = "Funding Information: The authors thank Arthur Yelon ({\'E}cole Polytechnique de Montr{\'e}al) for Meyer-Neldel discussions over some years and for a critical reading of the manuscript. LM{\textquoteright}s research has been funded in part by grants from the US National Science Foundation (DMR-1006332) and the National Institutes of Health (R01 GM088403).",

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doi = "10.1007/s00706-012-0839-9",

language = "English (US)",

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T1 - Entropy-enthalpy compensation of biomolecular systems in aqueous phase

T2 - A dry perspective

AU - Movileanu, Liviu

AU - Schiff, Eric A.

N1 - Funding Information: The authors thank Arthur Yelon (École Polytechnique de Montréal) for Meyer-Neldel discussions over some years and for a critical reading of the manuscript. LM’s research has been funded in part by grants from the US National Science Foundation (DMR-1006332) and the National Institutes of Health (R01 GM088403).

PY - 2013/1

Y1 - 2013/1

N2 - We survey thermodynamic measurements on processes involving biological macromolecules in aqueous solution, which illustrate well the ubiquitous phenomenon of entropy-enthalpy compensation. The processes include protein folding/unfolding and ligand binding/unbinding, with compensation temperatures varying by about 50 K around an average near 293 K. We show that incorporating both near-exact entropy-enthalpy compensation (due to solvent relaxation) and multi-excitation entropy (from vibrational quanta) leads to a compensation temperature in water of about 230 K. We illustrate a general procedure for subtracting solvent and environment-related terms to determine the bare Gibbs free energy changes of chemical processes.

AB - We survey thermodynamic measurements on processes involving biological macromolecules in aqueous solution, which illustrate well the ubiquitous phenomenon of entropy-enthalpy compensation. The processes include protein folding/unfolding and ligand binding/unbinding, with compensation temperatures varying by about 50 K around an average near 293 K. We show that incorporating both near-exact entropy-enthalpy compensation (due to solvent relaxation) and multi-excitation entropy (from vibrational quanta) leads to a compensation temperature in water of about 230 K. We illustrate a general procedure for subtracting solvent and environment-related terms to determine the bare Gibbs free energy changes of chemical processes.

KW - Biological macromolecules

KW - Entropy-enthalpy compensation

KW - Hydrophobic interactions

KW - Macromolecules

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DO - 10.1007/s00706-012-0839-9

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SN - 0026-9247

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JO - Monatshefte fur Chemie

JF - Monatshefte fur Chemie

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ER -

Entropy-enthalpy compensation of biomolecular systems in aqueous phase: A dry perspective

Abstract

Keywords

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