Cited Article: Hummer, G. Water conduction through the hydrophobic channel of a carbon nanotube
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Title:
Interfacial Free Energy Governs Single Polystyrene Chain Collapse in Water and Aqueous Solutions
Authors:
Li, ITS; Walker, GC
Author Full Names:
Li, Isaac T. S.; Walker, Gilbert C.
Source:
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 132 (18): 6530-6540 MAY 12 2010
Language:
English
Document Type:
Article
KeyWords Plus:
MOLECULE FORCE SPECTROSCOPY; HYDROPHOBIC POLYMER COLLAPSE; MECHANICAL UNFOLDING PATHWAY; SURFACE-TENSION; INTERMOLECULAR INTERACTIONS; POOR SOLVENT; PRESSURE DENATURATION; DISPERSION FORCES; PROTEINS; TRANSITION
Abstract:
The hydrophobic interaction is significantly responsible for driving protein folding and self-assembly. To understand it, the thermodynamics, the role of water structure, the dewetting process surrounding hydrophobes, and related aspects have undergone extensive investigations. Here, we examine the hypothesis that polymer-solvent interfacial free energy is adequate to describe the energetics of the collapse of a hydrophobic homopolymer chain at fixed temperature, which serves as a much simplified model for studying the hydrophobic collapse of a protein. This implies that changes in polymer-solvent interfacial free energy should be directly proportional to the force to extend a collapsed polymer into a bad solvent. To test this hypothesis, we undertook single-molecule force spectroscopy on a collapsed, single, polystyrene chain in water-ethanol and water-salt mixtures where we measured the monomer solvation free energy from an ensemble average conformations. Different proport!
ions within the binary mixture were used to create solvents with different interfacial free energies with polystyrene. In these mixed solvents, we observed a linear correlation between the interfacial free energy and the force required to extend the chain into solution, which is a direct measure of the solvation free energy per monomer on a single chain at room temperature. A simple analytical model compares favorably with the experimental results. This knowledge supports a common assumption that explicit water solvent may not be necessary for cases whose primary concerns are hydrophobic interactions and hydrophobic hydration.
Reprint Address:
Walker, GC, Univ Toronto, Dept Chem, Toronto, ON M5S 3H6, Canada.
Research Institution addresses:
[Li, Isaac T. S.; Walker, Gilbert C.] Univ Toronto, Dept Chem, Toronto, ON M5S 3H6, Canada
E-mail Address:
gwalker@chem.utoronto.ca
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Cited Reference Count:
95
Times Cited:
0
Publisher:
AMER CHEMICAL SOC; 1155 16TH ST, NW, WASHINGTON, DC 20036 USA
Subject Category:
Chemistry, Multidisciplinary
ISSN:
0002-7863
DOI:
10.1021/ja101155h
IDS Number:
593IB
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