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: 22] contact us to make corrections & updates to this data

Expand   Compare Data
compare with other measurements for proteins in this SCOP Family (1)

Expand   Protein Data
Protein Name Immunoglobulin light chain-binding domain of protein L (Protein L)
Oligomeric State Monomer
Folding Mechanism Not characterised
Intermediates 0
Phi Pattern No phi value analysis
SCOP Class Alpha+Beta   |   goto SCOP
SCOP Family Immunoglobulin-binding domains   |   goto SCOP

Expand   Construct Data
Species Peptostreptococcus magnus (Peptostreptococcus magnus)

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Sequence MHHHHHHAMEEVTIKANLIFANGSTQTAEFKGTFEKATSEAYAYADTLKK
DNGEWTVDVADKGYTLNIKFAG

Blast PFD  |  Blast NCBI NR
Length 72
Molecular Weight 8021.89Da
Fusion N-terminal hexahistidine
PDB ID 2PTL   |   goto PDB  
PDB Resolution NMR
Chain Chain 1 (NMR)
Residues 18 - 77
SCOP ID 54363   |   goto SCOP
UniProt ID Q51912_PEPMA   |   goto UniProt
Relative Contact Order 13.89

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 22
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)
-3.25 ± 0.1 4.1 ± 0.09 2.08 ± 0.05 -6.38 ± 0.19
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 -8.1 ± 0.4 19.9 ± 0.9
Probe Far-UV Circular Dichroism  what is this?
Pertubation Denaturant  what is this?
Technique GdnHCl
Instrument Aviv titrating Circular Di Spectrometer
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)
ND ND 0.03877 ± 0.00019 (0M) -3.25 ± 0.1 (0M) ND 2.08 ± 0.05
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)
ND ND 60.34 ± 0.24 4.1 ± 0.09 ND -6.38 ± 0.19
Probe Trp Fluorescence  what is this?
Pertubation Denaturant  what is this?
Technique GdnHCl
Instrument Applied Photophysics standard 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 The small size of the protein reduces the complexity of the folding problem, and the lack of disulfide bonds and proline residues simplifies data analysis. The solution structure of protein L, determined by high-resolution NMR (Wikstrom et al., 1994, 1993), consists of a single helix packed against a four-stranded beta sheet.
Construct Notes
Equilibrium Notes Protein L and FynSH3 These proteins were expressed and purified as previously described (Scalley et al. 1997; Maxwell and Davidson 1998) and employed without cleavage of the his-tag. Kinetics were monitored via tryptophan fluorescence (excitation 280 nm, emission >320 nm) on an APP stopped-flow fluorimeter. Equilibrium unfolding was monitored via CD at 220 nm on an Aviv titrating CD spec- trometer with a 2-min equilibration time. Both proteins have previously been established to fold via an apparently two-state process (Scalley et al. 1997; Plaxco et al. 1998a) (M.A.R., K.W.P.).
Kinetic Notes Protein L and FynSH3 These proteins were expressed and purified as previously described (Scalley et al. 1997; Maxwell and Davidson 1998) and employed without cleavage of the his-tag. Kinetics were monitored via tryptophan fluorescence (excitation 280 nm, emission >320 nm) on an APP stopped-flow fluorimeter. Equilibrium unfolding was monitored via CD at 220 nm on an Aviv titrating CD spec- trometer with a 2-min equilibration time. Both proteins have previously been established to fold via an apparently two-state process (Scalley et al. 1997; Plaxco et al. 1998a) (M.A.R., K.W.P.).
Comments view comments on this measurement

contact us to make corrections & updates to this data