Journal
PROTEIN SCIENCE
Volume 14, Issue 3, Pages 602-616Publisher
WILEY
DOI: 10.1110/ps.041205405
Keywords
two-state; protein folding; kinetics; chevron plots; equilibrium
Categories
Funding
- NIGMS NIH HHS [R01 GM070941, GM62868-01A2, R29 GM055694, R01 GM059663, R01 GM050945, R01 GM062868, GM50945, GM55694, GM70941, GM59663, R01 GM055694] Funding Source: Medline
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Recent years have seen the publication of both empirical and theoretical relationships predicting the rates with which proteins fold. Our ability to test and refine these relationships has been limited, however, by a variety of difficulties associated with the comparison of folding and unfolding rates, thermodynamics, and structure across diverse sets of proteins. These difficulties include the wide, potentially confounding range of experimental conditions and methods employed to date and the difficulty of obtaining correct and complete sequence and structural details for the characterized constructs. The lack of a single approach to data analysis and error estimation, or even of a common set of units and reporting standards, further hinders comparative studies of folding. In an effort to overcome these problems, we define here a consensus set of experimental conditions (25degreesC at pH 7.0, 50 mM buffer), data analysis methods, and data reporting standards that we hope will provide a benchmark for experimental studies. We take the first step in this initiative by describing the folding kinetics of 30 apparently two-state proteins or protein domains under the consensus conditions. The goal of our efforts is to set uniform standards for the experimental community and to initiate an accumulating, self-consistent data set that will aid ongoing efforts to understand the folding process.
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