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• W2053111993 abstract "Recent experimental work on fast protein folding brings about an intriguing paradox. Microsecond-folding proteins are supposed to fold near or at the folding speed limit (downhill folding), but yet their folding behavior seems to comply with classical two-state analyses, which imply the crossing of high free energy barriers. However, close inspection of chemical and thermal denaturation kinetic experiments in fast-folding proteins reveals systematic deviations from two-state behavior. Using a simple one-dimensional free energy surface approach we find that such deviations are indeed diagnostic of marginal folding barriers. Furthermore, the quantitative analysis of available fast-kinetic data indicates that many microsecond-folding proteins fold downhill in native conditions. All of these proteins are then promising candidates for an atom-by-atom analysis of protein folding using nuclear magnetic resonance.1 We also find that the diffusion coefficient for protein folding is strongly temperature dependent, corresponding to an activation energy of approximately 1 kJ.mol-1 per protein residue. As a consequence, the folding speed limit at room temperature is about an order of magnitude slower than the approximately 1 micros estimates from high-temperature T-jump experiments. Our analysis is quantitatively consistent with the available thermodynamic and kinetic data on slow two-state folding proteins and provides a straightforward explanation for the apparent fast-folding paradox." @default.
• W2053111993 created "2016-06-24" @default.
• W2053111993 creator A5047736259 @default.
• W2053111993 creator A5070803211 @default.
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• W2053111993 date "2007-04-10" @default.
• W2053111993 modified "2023-10-16" @default.
• W2053111993 title "Protein Folding Kinetics: Barrier Effects in Chemical and Thermal Denaturation Experiments" @default.
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• W2053111993 doi "https://doi.org/10.1021/ja0689740" @default.
• W2053111993 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2527040" @default.
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