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Detecting Selection on Protein Stability through Statistical Mechanical Models of Folding and Evolution

Kinetics and Thermodynamics of Membrane Protein Folding

Laboratory of Molecular Biophysics, Institute of Biochemistry and Biophysical Chemistry, University of Buenos Aires-CONICET, Buenos Aires 1113, Argentina
Author to whom correspondence should be addressed.
Biomolecules 2014, 4(1), 354-373;
Received: 31 December 2013 / Revised: 19 February 2014 / Accepted: 23 February 2014 / Published: 18 March 2014
(This article belongs to the Special Issue Protein Folding and Misfolding)
Understanding protein folding has been one of the great challenges in biochemistry and molecular biophysics. Over the past 50 years, many thermodynamic and kinetic studies have been performed addressing the stability of globular proteins. In comparison, advances in the membrane protein folding field lag far behind. Although membrane proteins constitute about a third of the proteins encoded in known genomes, stability studies on membrane proteins have been impaired due to experimental limitations. Furthermore, no systematic experimental strategies are available for folding these biomolecules in vitro. Common denaturing agents such as chaotropes usually do not work on helical membrane proteins, and ionic detergents have been successful denaturants only in few cases. Refolding a membrane protein seems to be a craftsman work, which is relatively straightforward for transmembrane β-barrel proteins but challenging for α-helical membrane proteins. Additional complexities emerge in multidomain membrane proteins, data interpretation being one of the most critical. In this review, we will describe some recent efforts in understanding the folding mechanism of membrane proteins that have been reversibly refolded allowing both thermodynamic and kinetic analysis. This information will be discussed in the context of current paradigms in the protein folding field. View Full-Text
Keywords: membrane proteins; thermodynamic stability; urea; guanidine hydrochloride; sodium dodecyl sulfate membrane proteins; thermodynamic stability; urea; guanidine hydrochloride; sodium dodecyl sulfate
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MDPI and ACS Style

Roman, E.A.; González Flecha, F.L. Kinetics and Thermodynamics of Membrane Protein Folding. Biomolecules 2014, 4, 354-373.

AMA Style

Roman EA, González Flecha FL. Kinetics and Thermodynamics of Membrane Protein Folding. Biomolecules. 2014; 4(1):354-373.

Chicago/Turabian Style

Roman, Ernesto A., and F. Luis González Flecha. 2014. "Kinetics and Thermodynamics of Membrane Protein Folding" Biomolecules 4, no. 1: 354-373.

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