Molecular crowding effects on protein stability.

Florin Despa; Dennis P. Orgill; Raphael C. Lee

doi:10.1196/annals.1363.005

Molecular crowding effects on protein stability.

Florin Despa, Dennis P. Orgill, Raphael C. Lee

Research output: Contribution to journal › Review article › peer-review

56 Scopus citations

Abstract

The volume fraction occupied by the dry matter of the cell can be as large as 40%, of which more than half (approximately 60%) are proteins. Thus, cellular proteins and protein assemblies occupy a large volume that can have a profound effect on their own native-state stabilities and on their unfolding/refolding rates. In addition, macromolecular crowding can change the properties of a significant fraction of the water in the cell. We review features of the molecular crowding effect which are relevant for describing the microscopic mechanism of thermal injuries.

Original language	English
Pages (from-to)	54-66
Number of pages	13
Journal	Annals of the New York Academy of Sciences
Volume	1066
DOIs	https://doi.org/10.1196/annals.1363.005
State	Published - Mar 1 2006

ASJC Scopus subject areas

General Neuroscience
General Biochemistry, Genetics and Molecular Biology
History and Philosophy of Science

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AB - The volume fraction occupied by the dry matter of the cell can be as large as 40%, of which more than half (approximately 60%) are proteins. Thus, cellular proteins and protein assemblies occupy a large volume that can have a profound effect on their own native-state stabilities and on their unfolding/refolding rates. In addition, macromolecular crowding can change the properties of a significant fraction of the water in the cell. We review features of the molecular crowding effect which are relevant for describing the microscopic mechanism of thermal injuries.

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JO - Annals of the New York Academy of Sciences

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Molecular crowding effects on protein stability.

Abstract

ASJC Scopus subject areas

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