Effects of Crowding on the thermal stability of heterogeneous protein solutions
Effects of Crowding on the thermal stability of heterogeneous protein solutions
Engineering Village 2
? 2006 Elsevier Inc
Accession number: 8999814
Title: Effects of Crowding on the thermal stability of heterogeneous protein solutions
Authors: Despa, F.1 ; Orgill, D.P.; Lee, R.C.
Author affiliation: 1 Dept. of Surg., Chicago Univ., IL, USA
Serial title: Annals of Biomedical Engineering
Abbreviated serial title: Ann. Biomed. Eng. (USA)
Volume: 33
Issue: 8
Publication date: Aug. 2005
Pages: 1125-31
Language: English
ISSN: 0090-6964
CODEN: ABMECF
Document type: Journal article (JA)
Publisher: Kluwer Academic/Plenum Publishers
Country of publication: USA
Material Identity Number: I369-2005-009
Abstract: Crowding can substantially affect the transition of a protein between its native (N) and unfolded (U) states via volume exclusion effects. Also, it influences considerably the aggregation (A) of unfolded proteins. To examine the details, we developed an approach for computing the kinetic rates of the process N?U?A in which the concentration of the protein is explicitly taken into account. We then compute the relative change with temperature of the protein denaturation for various fractional volume occupancies and partition of proteins in solution. The analysis indicates that, in protein solutions in which the average distance between proteins is comparable with the radius of gyration of an unfolded protein, steric effects increase the stability of the proteins which are in compact, native states. In heterogeneous protein solutions containing various types of proteins with different thermal stabilities, the unfolding of the most thermolabile proteins will increase the stability of the other proteins. The results shed light on the way proteins change the thermal stability of a cell as they unfold and aggregate. This study may be valuable in questions related to the dynamics of thermal injuries
Number of references: 38
Inspec controlled terms: biochemistry - molecular biophysics - proteins - thermal stability
Uncontrolled terms: crowding effects - thermal stability - heterogeneous protein solutions - protein transition - volume exclusion effects - kinetic rates - protein concentration - protein denaturation - fractional proteins volume - proteins partition - gyration - unfolded protein - steric effects - proteins stability - thermolabile proteins - thermal injury dynamics - Lumry-Eyring model
Inspec classification codes: A8715B Biomolecular structure, configuration, conformation, and active sites - A8715H Biomolecular dynamics, molecular probes, molecular pattern recognition - A8715D Physical chemistry of biomolecular solutions; condensed states - A3620C Macromolecular conformation (statistics and dynamics)
Treatment: Experimental (EXP)
Discipline: Physics (A)
DOI: 10.1007/s10439-005-5780-8
Database: Inspec
Copyright 2006, The Institution of Engineering and Technology
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