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

Expand   Compare Data
compare with other measurements for this protein (204)compare with other measurements for proteins in this SCOP Family (204)

Expand   Protein Data
Protein Name Chymotrypsin Inhibitor 2 (CI2)
Oligomeric State Monomer
Folding Mechanism Nucleation-condensation
Intermediates 0
Phi Pattern CI2
SCOP Class Alpha+Beta   |   goto SCOP
SCOP Family CI-2 family of serine protease inhibitors   |   goto SCOP

Expand   Construct Data
Species Barley (Hordeum vulgare)

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Sequence MLKTEWPELVGKSVEEAKKVILQDKPEAQIIVLPVGTIVTMEYRIDRVRL
FVDKLDNIAQVPRVG

Blast PFD  |  Blast NCBI NR
Length 66
Molecular Weight 7398.78Da
Fusion None
PDB ID 2CI2   |   goto PDB  
PDB Resolution 2Å
Chain A
Residues 20 - 83
SCOP ID 54659   |   goto SCOP
UniProt ID ICI2_HORVU   |   goto UniProt
Relative Contact Order 15

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 10
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)
-10.33 ± 0.56 5.75 ± 17 4.2 ± 0.25 -5.7 ± 0.18
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 -8.3 ± 0.3 32.5 ± 1.4
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)
4.1 6.6 0.0000330 ± 0.0000050 (0M) -10.33 ± 0.56 (0M) ND 4.2 ± 0.25
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)
0.8 3.7 314.19 ± 3794629963.22 5.75 ± 17 ND -5.7 ± 0.18
Probe Far-UV Circular Dichroism  what is this?
Pertubation Denaturant  what is this?
Technique GdnHCl
Instrument Bio-Logic SFM4/QFM4 Stopped-flow Fluorometer  what is this?
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 folding of CI2 is simplified by the lack of disulphide bridges and cis-peptidyl-prolyl bonds in the native state. The protein consists of a single domain (or module) that does not have readily discernible substructures that make interactions primarily within themselves. Previous studies have established that the folding and unfolding of wild-type CI2 and a range of mutants conform to a single two-state model under both equilibrium and non-equilibrium conditions (Jackson & Fersht, 1991, Jackson et al., 1993). In particular, the ratio of rate constants for unfolding and refolding give the correct equilibrium constant for unfolding (Jackson & Fersht, 1991a; Jackson et al., 1993b).
Construct Notes
Equilibrium Notes CI2. The equilibrium unfolding of the protein was characterized with an Aviv titrating CD spectrometer set at 220 nm. Equilibration time was 2 minutes.
Kinetic Notes CI2. Stopped-flow kinetic folding and unfolding were performed with a Biologic SFM4 (Claix, France) machine. Rate constants were determined by monitoring the change in the fluorescence signal. The excitation wavelength was 280 nm, and emission was collected at 320 nm. The faster measurable kinetic phase, which appears to represent a two-state, non-proline-limited phase (Jackson & Fersht, 1991), was used in this analysis.
Comments view comments on this measurement

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