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

Expand   Compare Data
compare with other measurements for this protein (2)compare with other measurements for proteins in this SCOP Family (4)

Expand   Protein Data
Protein Name Acyl Coenzyme A Binding Protein (ACBP)
Oligomeric State Monomer
Folding Mechanism Nucleation-condensation
Intermediates 0
Phi Pattern No phi value analysis
SCOP Class Alpha   |   goto SCOP
SCOP Family Acyl-Co A Binding Protein   |   goto SCOP

Expand   Construct Data
Species Rat (Rattus norvegicus)

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Sequence MSQADFDKAAEEVKRLKTQPTDEEMLFIYSHFKQATVGDVNTDRPGLLDL
KGKAKWDSWNKLKGTSKENAMKTYVEKVEELKKKYGI

Blast PFD  |  Blast NCBI NR
Length 87
Molecular Weight 10009.4Da
Fusion None
PDB ID 1NTI   |   goto PDB  
PDB Resolution NMR
Chain Any chain
Residues 1 - 86
SCOP ID 47030   |   goto SCOP
UniProt ID ACBP_RAT   |   goto UniProt
Relative Contact Order 12.18

Expand   Publication Data
Publication Kragelund BB et al (1996) Fast and one-step folding of closely and distantly related homologous proteins of a four-helix bundle family., J. Mol. Biol. 256, 187-200  goto pubmed
Data type in publication Equilibrium & Kinetic   |   view other data in this publication

Expand   Graphical Analysis Data
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)
0.5 1.78 ± 0.02 14.23 ± 0.29 25.31 ± 1.97
Probe Trp Fluorescence  what is this?
Pertubation Denaturant  what is this?
Technique GdnHCl
Instrument Perkin-Elmer LS50B Luminescence Spectrometer
Temperature 298K
pH 5.3
Buffer 0.02M Acetate
Protein Concentration 0.0040M

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 0.0066710 ± 0.0000030 (0M) -5.01 ± 0.03 (0M) 1.06 ± 0.04 ND
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 395.44 ± 3.35 5.98 ± 0.13 2.31 ± 0.06 ND
Other Kinetic Data
[Denaturant] 50%
(M)		 KD-N mD-N ∆GD-NH2O Kinetic βT Kinetic Unfolding βT Kinetic Folding βT Equilibrium Unfolding βT Equilibrium Folding
ND ND ND ND ND 0.69 ND ND
Probe Trp Fluorescence  what is this?
Pertubation Denaturant  what is this?
Technique GdnHCl
Instrument Bio-Logic SFM4/QFM4 Stopped-flow Fluorometer  what is this?
Temperature 298K
pH 5.3
Buffer 0.02M Acetate
Protein Concentration 0.0040M
Unfolding Fit Linear
Refolding Fit Linear

Expand   Notes & Comments on this measurement
Measurement Notes The folding reaction of ACBP is very fast even at 5 deg. C (Kragelund et al., 1995), which has imposed limits to the measurements of both the folding and unfolding rates at low and high concentrations of denaturant. Any intermediates that would be stabilised at low concentration of denaturant would under the present conditions not be detected. Measurements were possible at a residual denaturant concentration as low as 0.56 M. The equilibrium unfolding curve suggests a cooperative folding-unfolding process without any detectable intermediate states. The slope of the curve at the transition, the m-value, was typically determined with some uncertainty and with a rather dissatisfying reproducibility, quite possibly due to a small instability in temperature. Nevertheless, the m-value determined at equilibrium was shown to be in good agreement with that obtained from fits to the kinetics data, which are determined with relatively small uncertainties .The more precise values for the free energies of unfolding, DeltaGH2O, obtained from the kinetic experiments were used for comparisons.
Protein Notes Four-helix boundle motif where the four alpha helices, A1 to A4 are arranged in a left handed up-down-down-up orientation with an overhand connection between A2 and A3. The helices interact mainly through hydrophobic interactions.
Construct Notes The Rat structure has not been solved. The PDB refers to the NMR structure of Bovine ACBP.
Equilibrium Notes Samples allowed to equilibrate for one hour. Fluorescence spectra were recorded between 300 and 400 nm, and the excitation wavelength was 280 nm
Kinetic Notes The refolding reactions were followed using a Biologic SFM4 stopped-flow module with a Perkin-Elmer Lambda 9 spectrophotometer connected via an optical fibre (Fiberguide Industries) as light source with an excitation wavelength of 280 nm. Total emission above 320 nm was detected by a Hamamatzu R-376 photomultiplier connected to a Biologic PMS200 photomultiplier detection unit. A cut-off filter blocking transmission below 295 nm was inserted in front of the photomultiplier. were performed at 278 K. The folding and unfolding kinetics were fitted to exponentials using in-house programs providing uncertainties which represent 95% confidence intervals. The influence of GuHCl on the rates of folding and unfolding were determined by fitting data to a two-state reaction (Jackson et al., 1993b). Also, [GuHCl]50% values were obtained directly by fitting the data to the following equation: ln k = ln[k50%(exp(-mkf([GuHCl] - [GuHCl]50%)) + exp(mku([GuHCl] - [GuHCl]50%)))] where mkf and mku are the slopes, representing the dependence of the change in free energy on the concentration of the denaturant, and k50% is the rate of folding at the midpoint of the transition. The stabilities of the variants of ACBP were related to that of bovine ACBP.
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