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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)
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  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: 11] contact us to make corrections & updates to this data

Expand   Protein Data
Protein Name Ribosomal protein L9 C-domain (CTL9)
Oligomeric State Monomer
Folding Mechanism Not characterised
Intermediates 0
Phi Pattern No phi value analysis
SCOP Class Alpha+Beta   |   goto SCOP
SCOP Family Ribosomal protein L9 C-domain   |   goto SCOP

Expand   Construct Data
Species Bacillus stearothermophilus (Bacillus stearothermophilus)

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Sequence AAEELANAKKLKEQLEKLTVTIPAKAGEGGRLFGSITSKQIAESLQAQHG
LKLDKRKIELADAIRALGYTNVPVKLHPEVTATLKVHVTEQK

Blast PFD  |  Blast NCBI NR
Length 93
Molecular Weight 9963.59Da
Fusion None
PDB ID 1DIV   |   goto PDB  
PDB Resolution NMR
Chain Any chain
Residues 58 - 149
SCOP ID 40692   |   goto SCOP
UniProt ID RL9_BACST   |   goto UniProt
Relative Contact Order 13.76

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 11
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)
-7.85 ± 0.37 3.27 ± 0.06 1.38 ± 0.1 -3.09 ± 0.04
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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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 -4.4 ± 0.1 27.2 ± 0.3
Probe Trp Fluorescence  what is this?
Pertubation Denaturant  what is this?
Technique Urea
Instrument Fluorolog-3 Spectrofluorometer  what is this?
Temperature 298K
pH 8
Buffer 0.02M Phosphate
Protein Concentration 0.02M

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)
6.8 7.9 0.000390 ± 0.000027 (0M) -7.85 ± 0.37 (0M) ND 1.38 ± 0.1
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)
0.9 6.3 26.31 ± 0.05 3.27 ± 0.06 ND -3.09 ± 0.04
Probe Trp Fluorescence  what is this?
Pertubation Denaturant  what is this?
Technique Urea
Instrument Applied Photophysics SX.18MV Stopped-flow fluorimeter
Temperature 298K
pH 8
Buffer 0.02M Phosphate
Protein Concentration 0.02M
Unfolding Fit Linear
Refolding Fit Linear

Expand   Notes & Comments on this measurement
Measurement Notes
Protein Notes
Construct Notes Residues 1-57 in PDB entry 1DIV are highly disordered (B factor >100). Recalculating the absolute contact order using residues 58-149 gives a value of 12.8. Full length CO = 10.4
Equilibrium Notes CTL9. Maxwell et al, 2005. The protein was expressed and purified as described (Sato et al., 2001) and characterization under the conditions reported (Table 1) as described (Kuhlman et al., 1998; Sato and Raleigh, 2002; Sato, 2002). CTL9 was studied at pH 8.0 because the stability and folding rate are strongly pH dependent between pH 5 and pH 7.5. The protein is most stable above pH 7.5 (Sato & Raleigh, 2002; Sato, 2002). The chevron plot represents the faster of two phases. Previous reports indicate that the slower phase reflects proline isomerism (Sato & Raleigh, 2002; Sato, 2002). Sato and Raleigh 2002: Denaturant-induced unfolding of CTL9 was followed by measuring CD and fluorescence signals. CD measurements were made using an AVIV 62A DS spectrometer equipped with a Peltier temperature control unit. CD signals at 222 nm were averaged for 30 seconds at a given denaturant concentration after a five-minute equilibration period. Fluorescence measurements were preformed using an ISA Fluorolog spectrometer with an excitation wavelength of 276 nm. Fluorescence signals at 305 (±2.0) nm were averaged for 30 seconds at each denaturation concentration after a five-minute equilibration period. The protein concentration was 20 microM.
Kinetic Notes CTL9. Maxwell et al, 2005: The protein was expressed and purified as described (Sato et al., 2001) and characterization under the conditions reported as described (Kuhlman et al., 1998; Sato and Raleigh, 2002; Sato, 2002). CTL9 was studied at pH 8.0 because the stability and folding rate are strongly pH dependent between pH 5 and pH 7.5. The protein is most stable above pH 7.5 (Sato & Raleigh, 2002; Sato, 2002). The chevron plot represents the faster of two phases. Previous reports indicate that the slower phase reflects proline isomerism (Sato & Raleigh, 2002; Sato, 2002). Sato and Raleigh 2002: Fluorescence detected and CD-detected stopped-flow experiments were performed using an Applied Photophysics SX18MV stopped-flow reaction analyzer, and an AVIV stopped-flow CD spectrometer model 202SF respectively. Fluorescence signals of CTL9 were measured with an excitation wavelength of 276 (±2) nm using a 305 nm cutoff filter. The CD signal at 222 nm was monitored during the reactions. For denaturation jump experiments, protein samples were denatured in a high concentration of denaturant and folding was initiated by an 11-fold dilution into lower concentrations of denaturant. Unfolding was initiated by an 11-fold dilution into higher concentrations of denaturant. The resulting curves were fit with a double-exponential function to obtain first-order rate constants for each phase.
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contact us to make corrections & updates to this data