Molecular crowding effects on protein stability.
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.
Despa
Florin
F
Department of Surgery, MC 6035, University of Chicago, Chicago, IL 60637, USA.
Orgill
Dennis P
DP
Lee
Raphael C
RC
D008433:Mathematics; D008958:Models, Molecular; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry / Q000378:metabolism; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
D011506:Proteins; D014867:Water