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

58 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

Access to Document

10.1196/annals.1363.005

Cite this

@article{eb4dbe4932e84a90a30d8fcba54e4090,

title = "Molecular crowding effects on protein stability.",

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.",

author = "Florin Despa and Orgill, \{Dennis P.\} and Lee, \{Raphael C.\}",

year = "2006",

month = mar,

day = "1",

doi = "10.1196/annals.1363.005",

language = "English",

volume = "1066",

pages = "54--66",

}

TY - JOUR

T1 - Molecular crowding effects on protein stability.

AU - Despa, Florin

AU - Orgill, Dennis P.

AU - Lee, Raphael C.

PY - 2006/3/1

Y1 - 2006/3/1

N2 - 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.

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.

UR - https://www.scopus.com/pages/publications/33749054520

UR - https://www.scopus.com/pages/publications/33749054520#tab=citedBy

U2 - 10.1196/annals.1363.005

DO - 10.1196/annals.1363.005

M3 - Review article

C2 - 16533918

AN - SCOPUS:33749054520

SN - 0077-8923

VL - 1066

SP - 54

EP - 66

JO - Annals of the New York Academy of Sciences

JF - Annals of the New York Academy of Sciences

ER -

Molecular crowding effects on protein stability.

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this