Table 2. Characteristics of proteins with two-state kinetics

Table 1. Characteristics of proteins with multi-state kinetics

 Protein (or domain) namearticle
1En-HD Mayor, U. Johnson, C.M., Daggett, V. & Fersht, A.R. Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation. Proc. Natl. Acad. Sci. USA 97, 13518-13522 (2000).
2434 Cro Laurents DV, Corrales S, Elias-Arnanz M, Sevilla P, Rico M, Padmanabhan S. 2000. Folding kinetics of phage 434 Cro protein. Biochemistry 39:13963-13973.
3Ubiquitin Parker MJ, Marqusee S. 1999. The cooperativity of burst phase reactions explored. J Mol Biol 293:1195-1210.
4Im7 Ferguson N, Capaldi AP, James R, Kleanthous C, Radford SE. 1999. Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9. J Mol Biol 286:1597-1608.
5HypF-N Calloni, G. et al. Comparison of the folding processes of distantly related proteins. Importance of hydrophobic content in folding. J. Mol. Biol. 330, 577-591 (2003).
6TI I27 Fowler SB, Clarke J. 2001. Mapping the Folding Pathway of an Immunoglobulin Domain. Structural Detail from Phi Value Analysis and Movement of the Transition State. Structure (Camb ) 9:355-366.
7Barstar Schreiber G, Fersht AR. 1993. The refolding of cis- and trans-peptidylprolyl isomers of barstar. Biochemistry 32:11195-11203.
8suc1 Schymkowitz JW, Rousseau F, Irvine LR, Itzhaki LS. 2000. The folding pathway of the cell-cycle regulatory protein p13suc1: clues for the mechanism of domain swapping. Structure Fold Des 8:89-100.
9CD2.D1 Parker MJ, Dempsey CE, Lorch M, Clarke AR. 1997. Acquisition of native beta-strand topology during the rapid collapse phase of protein folding. Biochemistry 36:13396-13405.
10Barnase Matouschek A, Kellis JT, Jr., Serrano L, Bycroft M, Fersht AR. 1990. Transient folding intermediates characterized by protein engineering. Nature 346:440-445.
11Villin 14T Choe SE, Matsudaira PT, Osterhout J, Wagner G, Shakhnovich EI. 1998. Folding kinetics of villin 14T, a protein domain with a central beta- sheet and two hydrophobic cores. Biochemistry 37:14508-14518.
12p16 Tang KS, Guralnick BJ, Wang WK, Fersht AR, Itzhaki LS. 1999. Stability and folding of the tumour suppressor protein p16. J Mol Biol 285:1869-1886.
13ILBP Dalessio PM, Ropson IJ. 2000. Beta-sheet proteins with nearly identical structures have different folding intermediates. Biochemistry 39:860-871.
14CheY Munoz V, Lopez EM, Jager M, Serrano L. 1994. Kinetic characterization of the chemotactic protein from Escherichia coli, CheY. Kinetic analysis of the inverse hydrophobic effect. Biochemistry 33:5858-5866.
15IFABP Burns LL, Dalessio PM, Ropson IJ. 1998. Folding mechanism of three structurally similar beta-sheet proteins. Proteins 33:107-118.
16CRBPII Burns LL, Dalessio PM, Ropson IJ. 1998. Folding mechanism of three structurally similar beta-sheet proteins. Proteins 33:107-118.
17CRABPI Burns LL, Dalessio PM, Ropson IJ. 1998. Folding mechanism of three structurally similar beta-sheet proteins. Proteins 33:107-118.
18apoMb Cavagnero S, Dyson HJ, Wright PE. 1999. Effect of H helix destabilizing mutations on the kinetic and equilibrium folding of apomyoglobin. J Mol Biol 285:269-282.
19GroEL(191-345) Golbik R, Zahn R, Harding SE, Fersht AR. 1998. Thermodynamic stability and folding of GroEL minichaperones. J Mol Biol 276:505-515.
20RNase HI Parker MJ, Marqusee S. 1999. The cooperativity of burst phase reactions explored. J Mol Biol 293:1195-1210.
21DHFR Jennings PA, Finn BE, Jones BE, Matthews CR. 1993. A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: verification and refinement of a four-channel model. Biochemistry 32:3783-3789.
22T4L Parker MJ, Marqusee S. 1999. The cooperativity of burst phase reactions explored. J Mol Biol 293:1195-1210.
23N-terminal domain from PGK Parker MJ, Spencer J, Clarke AR. 1995. An integrated kinetic analysis of intermediates and transition states in protein folding reactions. J Mol Biol 253:771-786.
24C-terminal domain from PGK Parker MJ, Sessions RB, Badcoe IG, Clarke AR. 1996. The development of tertiary interactions during the folding of a large protein. Fold Des 1:145-156.
25Tryptophan syntase α subunit Goldberg ME, Semisotnov GV, Friguet B, Kuwajima K, Ptitsyn OB, Sugai S. 1990. An early immunoreactive folding intermediate of the tryptophan synthease beta 2 subunit is a 'molten globule'. FEBS Lett 263:51-56.
26Tryptophan syntase β subunit Goldberg ME, Semisotnov GV, Friguet B, Kuwajima K, Ptitsyn OB, Sugai S. 1990. An early immunoreactive folding intermediate of the tryptophan synthease beta 2 subunit is a 'molten globule'. FEBS Lett 263:51-56.
27β-hairpin Munoz V, Thompson PA, Hofrichter J, Eaton WA. 1997. Folding dynamics and mechanism of beta-hairpin formation. Nature 390:196-199.
28α-helix Thompson PA, Eaton WA, Hofrichter J. 1997. Laser temperature jump study of the helix<==>coil kinetics of an alanine peptide interpreted with a 'kinetic zipper' model. Biochemistry 36:9200-9210.
29Trp-cage protein Qui L, Pabit SA, Roitberg AE, Hagen SJ. 2002. Smaller and faster: the 20-residue Trp-cage protein folds in 4 micros. J. Am. Chem. Soc. 124, 12952-12953.
30BBA5 Snow CD, Nguyen H., Pande VS, Gruebele M. 2002. Absolute comparison of simulated and experimental protein-folding dynamics. Nature 420:102-106.
31Pin WW domain Jager M, Nguyen H, Crane JC, Kelly JW, Gruebele M. 2001. The folding mechanism of a beta-sheet: the WW domain. J Mol Biol 311:373-393.
32HP36 Islam, S.A., Karplus, M. & Weaver, D.L. Application of the diffusion-collision model to the folding of three-helix bundle proteins. J. Mol. Biol. 318, 199-215 (2002).
33WW prototype Ferguson N, Johnson, CM, Macias M, Oschkinat H, Fersht A, Ultrafast folding of WW domains without structured aromatic clusters in the denatured state., PNAS, 2001, v. 98, p. 13002-13007
34FBP28 Ferguson N, Johnson, CV, Macias M, Oschkinat H, Fersht AR. 2001. Ultrafast folding of WW domains without structured aromatic clusters in the denatured state. PNAS 98:13002.
35YAP65 Ferguson N, Johnson, CM, Macias M, Oschkinat H, Fersht A, Ultrafast folding of WW domains without structured aromatic clusters in the denatured state., PNAS, 2001, v. 98, p. 13002-13007
36psbd41 Spector S, Raleigh DP. 1999. Submillisecond folding of the peripheral subunit-binding domain. J Mol Biol 293:763-768.
37Albumin-binding domain of protein PAB Wang T, Zhu Y, Gai F. 2004. Folding of a three-helix bundle at the folding speed limit. J.Phys.Chem.B 108:3694.
38c-Myb Gianni S, Guydosh NR, Khan F, Caldas TD, Mayor U, White GWN, DeMarco ML, Daggett V, Fersht AR, Unifying features in protein-folding mechanism., PNAS, 2003, v. 100, p. 13286-13291
39TRF1 Gianni S, Guydosh NR, Khan F, Caldas TD, Mayor U, White GWN, DeMarco ML, Daggett V, Fersht AR, Unifying features in protein-folding mechanism., PNAS, 2003, v. 100, p. 13286-13291
40Src SH3 Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallee-Belisle A, Main ER, Bemporad F, Qiu L, Teilum K, Vu ND, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai , Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Sci, 2005, v. 14, p. 602-616
41NTL9 Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallee-Belisle A, Main ER, Bemporad F, Qiu L, Teilum K, Vu ND, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai , Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Sci, 2005, v. 14, p. 602-616
42Protein G Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallee-Belisle A, Main ER, Bemporad F, Qiu L, Teilum K, Vu ND, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai , Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Sci, 2005, v. 14, p. 602-616
43Spectrin SH3 Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallee-Belisle A, Main ER, Bemporad F, Qiu L, Teilum K, Vu ND, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai , Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Sci, 2005, v. 14, p. 602-616
44Fyn SH3 Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallee-Belisle A, Main ER, Bemporad F, Qiu L, Teilum K, Vu ND, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai , Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Sci, 2005, v. 14, p. 602-616
45Abp1 SH3 Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallee-Belisle A, Main ER, Bemporad F, Qiu L, Teilum K, Vu ND, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai , Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Sci, 2005, v. 14, p. 602-616
46RAP1 Gianni S, Guydosh NR, Khan F, Caldas TD, Mayor U, White GWN, DeMarco ML, Daggett V, Fersht AR, Unifying features in protein-folding mechanism., PNAS, 2003, v. 100, p. 13286-13291
47BdpA Myers JK, Oas TG, Pre-organized secondary structure as an important determinant of fast protein folding., Nat Struct Biol, 2001, v. 8, p. 552-558
48Protein L Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallee-Belisle A, Main ER, Bemporad F, Qiu L, Teilum K, Vu ND, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai , Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Sci, 2005, v. 14, p. 602-616
49Sso7d Guerois R, Serrano L, The SH3-fold family: experimental evidence and prediction of variations in the folding pathways., JMB, 2000, v. 304, p. 967-982
50Ci2 Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallee-Belisle A, Main ER, Bemporad F, Qiu L, Teilum K, Vu ND, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai , Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Sci, 2005, v. 14, p. 602-616
51CspB Perl D, Welker C, Schindler T, Schroder K, Marahiel MA, Jaenicke R, Schmid FX, Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins., Nat Struct Biol, 1998, v. 5, p. 229-235
52CspB Perl D, Welker C, Schindler T, Schroder K, Marahiel MA, Jaenicke R, Schmid FX, Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins., Nat Struct Biol, 1998, v. 5, p. 229-235
53CspB Perl D, Welker C, Schindler T, Schroder K, Marahiel MA, Jaenicke R, Schmid FX, Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins., Nat Struct Biol, 1998, v. 5, p. 229-235
54EC298 Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallee-Belisle A, Main ER, Bemporad F, Qiu L, Teilum K, Vu ND, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai , Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Sci, 2005, v. 14, p. 602-616
55PsaE Ivankov, D.N. and Finkelstein, A.V. (2004) Prediction of protein folding rates from the amino acid sequence-predicted secondary structure. Proc Natl Acad Sci U S A, 101, 8942-8944
56CspA Reid KL, Rodriguez HM, Hillier BJ, Gregoret LM, Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA., Protein Sci, 1998, v. 7, p. 470-479
57ADAh2 Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallee-Belisle A, Main ER, Bemporad F, Qiu L, Teilum K, Vu ND, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai , Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Sci, 2005, v. 14, p. 602-616
58α3D Zhu Y, Alonso DO, Maki K, Huang CY, Lahr SJ, Daggett V, Roder H, DeGrado WF, Gai F, Ultrafast folding of alpha-3-D: a de novo designed three-helix bundle protein., PNAS, 2003, v. 100, p. 15486-15491
59GW1 Myers JK, Oas TG, Pre-organized secondary structure as an important determinant of fast protein folding., Nat Struct Biol, 2001, v. 8, p. 552-558
60raf RBD Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallee-Belisle A, Main ER, Bemporad F, Qiu L, Teilum K, Vu ND, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai , Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Sci, 2005, v. 14, p. 602-616
61λ-repressor Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallee-Belisle A, Main ER, Bemporad F, Qiu L, Teilum K, Vu ND, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai , Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Sci, 2005, v. 14, p. 602-616
62Im9 Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallee-Belisle A, Main ER, Bemporad F, Qiu L, Teilum K, Vu ND, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai , Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Sci, 2005, v. 14, p. 602-616
63HPr Van Nuland NA, Meijberg W, Warner J, Forge V, Scheek RM, Robillard GT, Dobson CM, Slow cooperative folding of a small globular protein HPr., Biochemistry, 1998, v. 37, p. 622-637
64ACBP Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallee-Belisle A, Main ER, Bemporad F, Qiu L, Teilum K, Vu ND, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai , Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Sci, 2005, v. 14, p. 602-616
65PI3-SH3 Guijarro JI, Morton CJ, Plaxco KW, Campbell ID, Dobson CM, Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy., JMB, 1998, v. 276, p. 657-667
66TNfn3 Clarke J, Hamill SJ, Johnson CM, Folding and stability of a fibronectin type III domain of human tenascin., JMB, 1997, v. 270, p. 771-778
679FNIII Plaxco KW, Spitzfaden C, Campbell ID, Dobson CM, A comparison of the folding kinetics and thermodynamics of two homologous fibronectin type III modules., JMB, 1997, v. 270, p. 763-770
68CTL9 FM, Kragelund BB, Michnick SW, Chiti F, Bai , Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Sci, 2005, v. 14, p. 602-616
69TWIg18’ Clarke J, Cota E, Fowler SB, Hamill SJ, Folding studies of immunoglobulin-like beta-sandwich proteins suggest that they share a common folding pathway., Structure Fold Des, 1999, v. 7, p. 1145-1153
70FNfn10 Plaxco KW, Spitzfaden C, Campbell ID, Dobson CM, A comparison of the folding kinetics and thermodynamics of two homologous fibronectin type III modules., JMB, 1997, v. 270, p. 763-770
71L23 Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallee-Belisle A, Main ER, Bemporad F, Qiu L, Teilum K, Vu ND, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai , Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Sci, 2005, v. 14, p. 602-616
72U1A Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallee-Belisle A, Main ER, Bemporad F, Qiu L, Teilum K, Vu ND, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai , Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Sci, 2005, v. 14, p. 602-616
73S6 FM, Kragelund BB, Michnick SW, Chiti F, Bai , Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Sci, 2005, v. 14, p. 602-616
74CT AcP Taddei N, Chiti F, Paoli P, Fiaschi T, Bucciantini M, Stefani M, Dobson CM, Ramponi G, Thermodynamics and kinetics of folding of common-type acylphosphotase: comparison to the highly homologous muscle isoenzyme., Biochemistry, 1999, v. 38, p. 2135-2142
75mAcP FM, Kragelund BB, Michnick SW, Chiti F, Bai , Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Sci, 2005, v. 14, p. 602-616
76SrcSH2 Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallee-Belisle A, Main ER, Bemporad F, Qiu L, Teilum K, Vu ND, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai , Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Sci, 2005, v. 14, p. 602-616
77cyt b562 Wittung-Stafshede P, Lee JC, Winkler JR, Gray HB, Cytochrome b562 folding triggered by electron transfer: approaching the speed limit for formation of a four-helix-bundle protein., PNAS, 1999, v. 96, p. 6587-6590
78R16 Scott KA, Batey S, Hooton KA, Clarke J, The folding of spectrin domains I: wild-type domains have the same stability but very different kinetic properties., JMB, 2004, v. 344, p. 195-205
79R17 Scott KA, Batey S, Hooton KA, Clarke J, The folding of spectrin domains I: wild-type domains have the same stability but very different kinetic properties., JMB, 2004, v. 344, p. 195-205
80FKBP Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallee-Belisle A, Main ER, Bemporad F, Qiu L, Teilum K, Vu ND, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai , Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Sci, 2005, v. 14, p. 602-616
81R15 Scott KA, Batey S, Hooton KA, Clarke J, The folding of spectrin domains I: wild-type domains have the same stability but very different kinetic properties., JMB, 2004, v. 344, p. 195-205
82CheW Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallee-Belisle A, Main ER, Bemporad F, Qiu L, Teilum K, Vu ND, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai , Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Sci, 2005, v. 14, p. 602-616
83CyPA Ikura T, Hayano T, Takahashi N, Kuwajima K, Fast folding of Escherichia coli cyclophilin A: a hypothesis of a unique hydrophobic core with a phenylalanine cluster., JMB, 2000, v. 297, p. 791-802
84VlsE Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallee-Belisle A, Main ER, Bemporad F, Qiu L, Teilum K, Vu ND, Edwards AM, Ruczinski I, Poulsen FM, Kragelund BB, Michnick SW, Chiti F, Bai , Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Sci, 2005, v. 14, p. 602-616