Microscopic mechanism for cold denaturation

Cristiano L. Dias; Tapio Ala-Nissila; Mikko Karttunen; Ilpo Vattulainen; Martin Grant

doi:10.1103/PhysRevLett.100.118101

Microscopic mechanism for cold denaturation

Cristiano L. Dias, Tapio Ala-Nissila, Mikko Karttunen, Ilpo Vattulainen, Martin Grant

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113 Scopus citations

Abstract

We elucidate the mechanism of cold denaturation through constant-pressure simulations for a model of hydrophobic molecules in an explicit solvent. We find that the temperature dependence of the hydrophobic effect induces, facilitates, and is the driving force for cold denaturation. The physical mechanism underlying this phenomenon is identified as the destabilization of hydrophobic contact in favor of solvent-separated configurations, the same mechanism seen in pressure-induced denaturation. A phenomenological explanation proposed for the mechanism is suggested as being responsible for cold denaturation in real proteins.

Original language	English (US)
Article number	118101
Journal	Physical Review Letters
Volume	100
Issue number	11
DOIs	https://doi.org/10.1103/PhysRevLett.100.118101
State	Published - Mar 18 2008
Externally published	Yes

All Science Journal Classification (ASJC) codes

General Physics and Astronomy

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10.1103/PhysRevLett.100.118101

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title = "Microscopic mechanism for cold denaturation",

abstract = "We elucidate the mechanism of cold denaturation through constant-pressure simulations for a model of hydrophobic molecules in an explicit solvent. We find that the temperature dependence of the hydrophobic effect induces, facilitates, and is the driving force for cold denaturation. The physical mechanism underlying this phenomenon is identified as the destabilization of hydrophobic contact in favor of solvent-separated configurations, the same mechanism seen in pressure-induced denaturation. A phenomenological explanation proposed for the mechanism is suggested as being responsible for cold denaturation in real proteins.",

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T1 - Microscopic mechanism for cold denaturation

AU - Dias, Cristiano L.

AU - Ala-Nissila, Tapio

AU - Karttunen, Mikko

AU - Vattulainen, Ilpo

AU - Grant, Martin

PY - 2008/3/18

Y1 - 2008/3/18

N2 - We elucidate the mechanism of cold denaturation through constant-pressure simulations for a model of hydrophobic molecules in an explicit solvent. We find that the temperature dependence of the hydrophobic effect induces, facilitates, and is the driving force for cold denaturation. The physical mechanism underlying this phenomenon is identified as the destabilization of hydrophobic contact in favor of solvent-separated configurations, the same mechanism seen in pressure-induced denaturation. A phenomenological explanation proposed for the mechanism is suggested as being responsible for cold denaturation in real proteins.

AB - We elucidate the mechanism of cold denaturation through constant-pressure simulations for a model of hydrophobic molecules in an explicit solvent. We find that the temperature dependence of the hydrophobic effect induces, facilitates, and is the driving force for cold denaturation. The physical mechanism underlying this phenomenon is identified as the destabilization of hydrophobic contact in favor of solvent-separated configurations, the same mechanism seen in pressure-induced denaturation. A phenomenological explanation proposed for the mechanism is suggested as being responsible for cold denaturation in real proteins.

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DO - 10.1103/PhysRevLett.100.118101

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VL - 100

JO - Physical Review Letters

JF - Physical Review Letters

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Microscopic mechanism for cold denaturation

Abstract

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