Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins

Karen L. Maxwell, David Wildes, Arash Zarrine-Afsar, Miguel A. De Los Rios, Andrew G. Brown, Claire T. Friel, Linda Hedberg, Jia Cherng Horng, Diane Bona, Erik J. Miller, Alexis Vallée-Bélisle, Ewan R.G. Main, Francesco Bemporad, Linlin Qiu, Kaare Teilum, Ngoc Diep Vu, Aled M. Edwards, Ingo Ruczinski, Flemming M. Poulsen, Birthe B. KragelundStephen W. Michnick, Fabrizio Chiti, Yawen Bai, Stephen J. Hagen, Luis Serrano, Mikael Oliveberg, Daniel P. Raleigh, Pernilla Wittung-Stafshede, Sheena E. Radford, Sophie E. Jackson, Tobin R. Sosnick, Susan Marqusee, Alan R. Davidson, Kevin W. Plaxco

Research output: Contribution to journalArticlepeer-review

164 Scopus citations


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 (25°C 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.

Original languageEnglish (US)
Pages (from-to)602-616
Number of pages15
JournalProtein Science
Issue number3
StatePublished - Mar 2005


  • Chevron plots
  • Equilibrium
  • Kinetics
  • Protein folding
  • Two-state

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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