The Protein Folding Database
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  Statistics
Version: 2.2
Last Update: 8-Jun-2007
Entries: 296
Proteins: 70
Families: 53
Species: 30
ϕ values: 230 (5 proteins)
Locations of visitors to this page
  Latest Additions
ACBP (3 WT)
FRB (6 WT)
CI2 (3 WT, 202 mutants)
HPr (1 WT, 4 mutants)
Im7 (1 WT)
En-HD (1 WT)
Im9 (2 WT)
Abp1 SH3 (1 WT)
CheW (1 WT)
U1A (1 WT)
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Fulton et al (2005) Nucleic Acids Res. 33:D279-283  |  Fulton et al (2007) Nucleic Acids Res. 35:D304-307 About PFD | Help | Glossary
Folding Data
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Note: A field with its data listed as "ND" denotes there is no data for that field.
[Measurement ID: 23] contact us to make corrections & updates to this data

Expand   Protein Data
Protein Name c-Raf1 RBD (raf RBD)
Oligomeric State Monomer
Folding Mechanism Not characterised
Intermediates 0
Phi Pattern No phi value analysis
SCOP Class Alpha+Beta   |   goto SCOP
SCOP Family Ras-binding domain, RBD   |   goto SCOP

Expand   Construct Data
Species Human (Homo sapiens)

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Sequence MGSNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLL
HEHKGKKARLDWNTDAASLIGEELQVDFLD

Blast PFD  |  Blast NCBI NR
Length 81
Molecular Weight 9059.58Da
Fusion None
PDB ID 1RFA   |   goto PDB  
PDB Resolution NMR
Chain Chain 1 (NMR)
Residues 55 - 132
SCOP ID 54265   |   goto SCOP
UniProt ID RAF1_HUMAN   |   goto UniProt
Relative Contact Order 15.43

Expand   Publication Data
Publication Maxwell KL et al (2005) Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Science 14, 602-616  goto pubmed
Data type in publication Equilibrium & Kinetic   |   view other data in this publication

Expand   Graphical Analysis Data
Chevron Plot chevron plot for measurement 23
unfolding & refolding data
ln(kuH2O)
(s-1)		 ln(kfH2O)
(s-1)		 m‡-N
(kJ mol-1 M-1)		 m‡-D
(kJ mol-1 M-1)
-2.77 ± 0.65 8.36 ± 0.12 1.03 ± 0.2 -3.39 ± 0.09
Notes on Chevron Plot Calculating
Contact Order Plot Data Acyl Coenzyme A Binding Protein Hypothetical protein YjbJ from Escherichia coli E colicin binding Immunity Protein 7 (ImmE7*) E colicin binding Immunity Protein 9 (ImmE9) Lambda C1 repressor, DNA-binding domain E colicin binding Immunity Protein 9 (ImmE9) Acyl Coenzyme A Binding Protein Acyl Coenzyme A Binding Protein Internalin B, C-terminal domain Apo-azurin Chemotaxis protein CheW Fyn proto-oncogene tyrosine kinase, SH3 domain Alpha-Spectrin SH3 Domain c-src tyrosine kinase SH3 Domain Actin binding protein 1 SH3 domain Activation Domain Of Human Procarboxypeptidase A2 Chymotrypsin Inhibitor 2 Ribosomal protein L9 C-domain FK-506 binding protein Ribosomal protein L23 Acylphosphatase Ribosomal protein L9 N-domain Immunoglobulin-binding protein G Immunoglobulin light chain-binding domain of protein L c-Raf1 RBD Ribosomal protein S6 c-src tyrosine kinase SH2 domain Spliceosomal U1A protein Ubiquitin FK-506 binding protein Chymotrypsin Inhibitor 2 Chymotrypsin Inhibitor 2
generated contact order graph

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Clicking on a data point will display folding data on that protein.
To view more data on a SCOP Class click on it's name in the legend.
Note: Mutant measurements do not have their data plotted on this graph, instead the data from wildtype is marked in red.

view notes on contact order

Expand   Equilibrium Data & Methods
Equilibrium Data
[Denaturant] Minimum
(M)		 [Denaturant] 50%
(M)		 mD-N (m)
(kJ mol-1 M-1)		 ∆GD-N (m)
(kJ mol-1)
ND ND -4.1 ± 0.5 26 ± 3
Probe Trp Fluorescence  what is this?
Pertubation Denaturant  what is this?
Technique Urea
Instrument Applied Photophysics SX.18MV Stopped-flow fluorimeter
Temperature 298K
pH 7
Buffer 0.05M Phosphate
Protein Concentration ND

Expand   Kinetic Data & Methods
Kinetic Unfolding Data
[Denaturant] Minimum
(M)		 [Denaturant] Maximum
(M)		 ku
(s-1)		 lnku
(s-1)		 mu
(M-1)		 m‡-N
(kJ mol-1 M-1)
5.76 8.01 0.06 ± 0.01 (0M) -2.77 ± 0.65 (0M) ND 1.03 ± 0.2
Kinetic Folding Data
[Denaturant] Minimum
(M)		 [Denaturant] Maximum
(M)		 kfH2O
(s-1)		 ln(kfH2O)
(s-1)		 mf
(M-1)		 m‡-D
(kJ mol-1 M-1)
0.92 5.61 4272.69 ± 30.8 8.36 ± 0.12 ND -3.39 ± 0.09
Probe Trp Fluorescence  what is this?
Pertubation Denaturant  what is this?
Technique Urea
Instrument Applied Photophysics SX.18MV Stopped-flow fluorimeter
Temperature 298K
pH 7
Buffer 0.05M Phosphate
Protein Concentration ND
Unfolding Fit Linear
Refolding Fit Linear

Expand   Notes & Comments on this measurement
Measurement Notes
Protein Notes
Construct Notes
Equilibrium Notes raf RBD. Maxwell et al, 2005. This protein was expressed, purified and characterized as previously described (Vallee-Belisle et al., 2004) save the characterization was performed under the conditions described. The most rapid refolding phase, which accounts for about 40% of the total amplitude at low denaturant concentrations, was well fitted to a two-state folding transition. Three additional, slower phases are resolved below 3 M urea. These exhibit rates, amplitudes and denaturant-dependencies similar to those previously (Vallee-Belisle et al., 2004) observed in GuHCl. In this previous study, rapid unfolding/refolding double-jump experiments suggested that the 3rd and 4th transitions could be attributed to non-prolyl and proline residues isomerizations, respectively. However, the nature of the second transition remains to be conclusively determined, since its amplitude remains constant even when the delay between unfolding and refolding is insufficient to equilibrate the cis-trans isomers of the unfolded state. (SWM, AVB)
Kinetic Notes raf RBD. Maxwell et al, 2005. This protein was expressed, purified and characterized as previously described (Vallee-Belisle et al., 2004) save the characterization was performed under the conditions described. The most rapid refolding phase, which accounts for about 40% of the total amplitude at low denaturant concentrations, was well fitted to a two-state folding transition. Three additional, slower phases are resolved below 3 M urea. These exhibit rates, amplitudes and denaturant-dependencies similar to those previously (Vallee-Belisle et al., 2004) observed in GuHCl. In this previous study, rapid unfolding/refolding double-jump experiments suggested that the 3rd and 4th transitions could be attributed to non-prolyl and proline residues isomerizations, respectively. However, the nature of the second transition remains to be conclusively determined, since its amplitude remains constant even when the delay between unfolding and refolding is insufficient to equilibrate the cis-trans isomers of the unfolded state. (SWM, AVB)
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contact us to make corrections & updates to this data