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Title

Exploiting the downhill folding regime via experiment

AuthorsMuñoz, Víctor; Sadqi, Mourad; Naganathan, Athi N. ; Sancho, David de
KeywordsFree energy
Molecular biophysics
Molecular force constants
Proteins
Thermodynamics
Issue Date13-Oct-2008
PublisherHuman frontier science program
CitationHFSP journal 3(6): 342-353 (2008)
AbstractTraditionally, folding experiments have been directed at determining equilibrium and relaxation rate constants of proteins that fold with two-state-like kinetics. More recently, the combination of free energy surface approaches inspired by theory with the discovery of proteins that fold in the downhill regime has greatly widened the battlefield for experimentalists. Downhill folding proteins cross very small or no free energy barrier at all so that all relevant partially folded conformations become experimentally accessible. From these combined efforts we now have tools to estimate the height of thermodynamic and kinetic folding barriers. Procedures to measure with atomic resolution the structural heterogeneity of conformational ensembles at varying unfolding degrees are also available. Moreover, determining the dynamic modes driving folding and how they change as folding proceeds is finally at our fingertips. These developments allow us to address via experiment fundamental questions such as the origin of folding cooperativity, the relationship between structure and stability, or how to engineer folding barriers. Moreover, the level of detail attained in this new breed of experiments should provide powerful benchmarks for computer simulations of folding and force-field refinement.
Description12 pages.-- PACS: 82.37.Rs; 87.14.E-
Publisher version (URL)http://dx.doi.org/10.2976/1.2988030
URIhttp://hdl.handle.net/10261/21896
DOI10.2976/1.2988030
ISSN1955-2068
Appears in Collections:(CIB) Artículos
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