Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins.
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 degrees 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.
Maxwell
Karen L
KL
Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada.
Wildes
David
D
Zarrine-Afsar
Arash
A
De Los Rios
Miguel A
MA
Brown
Andrew G
AG
Friel
Claire T
CT
Hedberg
Linda
L
Horng
Jia-Cherng
JC
Bona
Diane
D
Miller
Erik J
EJ
Vallée-Bélisle
Alexis
A
Main
Ewan R G
ER
Bemporad
Francesco
F
Qiu
Linlin
L
Teilum
Kaare
K
Vu
Ngoc-Diep
ND
Edwards
Aled M
AM
Ruczinski
Ingo
I
Poulsen
Flemming M
FM
Kragelund
Birthe B
BB
Michnick
Stephen W
SW
Chiti
Fabrizio
F
Bai
Yawen
Y
Hagen
Stephen J
SJ
Serrano
Luis
L
Oliveberg
Mikael
M
Raleigh
Daniel P
DP
Wittung-Stafshede
Pernilla
P
Radford
Sheena E
SE
Jackson
Sophie E
SE
Sosnick
Tobin R
TR
Marqusee
Susan
S
Davidson
Alan R
AR
Plaxco
Kevin W
KW
D001671:Biochemistry / Q000379:methods*; D003627:Data Interpretation, Statistical; D007700:Kinetics; D011489:Protein Denaturation; D017510:Protein Folding; D020673:Protein Renaturation; D011506:Proteins / Q000737:chemistry*
D011506:Proteins