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

Expand   Protein Data
Protein Name Acylphosphatase (mAcP)
Oligomeric State Monomer
Folding Mechanism Not characterised
Intermediates 0
Phi Pattern Barnase
SCOP Class Alpha+Beta   |   goto SCOP
SCOP Family Acylphosphatase-like   |   goto SCOP

Expand   Construct Data
Species Horse (Equus caballus)

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Sequence GSTAQSLKSVDYEVFGRVQGVCFRMYTEDEARKIGVVGWVKNTSKGTVTG
QVQGPEDKVNSMKSWLSKVGSPSSRIDRTNFSNEKTISKLEYSNFSIRY


Blast PFD  |  Blast NCBI NR
Length 100
Molecular Weight 11047.4Da
Fusion None
PDB ID 1APS   |   goto PDB  
PDB Resolution NMR
Chain Any chain
Residues 1 - 98
SCOP ID 54979   |   goto SCOP
UniProt ID ACYP2_HORSE   |   goto UniProt
Relative Contact Order 20.6

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 19
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)
-9 ± 0.35 -1.58 ± 0.18 4.12 ± 0.1 -1.27 ± 0.08
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 -5.3 ± 0.5 20.4 ± 0.2
Probe Trp Fluorescence  what is this?
Pertubation Denaturant  what is this?
Technique Urea
Instrument Perkin-Elmer LS55 Luminescence Spectrometer
Temperature 298K
pH 7
Buffer 0.05M TrisHCl
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 0.0001230 ± 0.0000080 (0M) -9 ± 0.35 (0M) ND 4.12 ± 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)
ND ND 0.2060 ± 0.0033 -1.58 ± 0.18 ND -1.27 ± 0.08
Probe Trp Fluorescence  what is this?
Pertubation Denaturant  what is this?
Technique Urea
Instrument Bio-Logic SFM-3 Stopped-flow Fluorometer  what is this?
Temperature 298K
pH 7
Buffer 0.05M TrisHCl
Protein Concentration ND
Unfolding Fit Linear
Refolding Fit Linear

Expand   Notes & Comments on this measurement
Measurement Notes
Protein Notes Muscle Acylphosphatase is a small monomeric alpha/beta protein that comprises mainly antiparallel beta sheets (segregated alpha and beta regions). Studies have demonstrated the protein to fold via a two state model and as such has been used for transition state analysis. Only the structures of horse and cow acylphosphatase have been solved, however folding studies have been performed on the human protein. Data communicated by Francesco Bemporad and Fabrizio Chiti, University of Florence, 4/2/05 Also published in Maxwell et al 2005
Construct Notes
Equilibrium Notes mAcP. Maxwell et al 2005. The human protein was expressed and purified as described previously (Taddei et al., 1996). Kinetic unfolding/refolding was followed using a Bio-logic SFM-3 stopped-flow fluorimeter, with excitation at 280 nm and a bandpass filter to monitor emitted fluorescence above 320 nm under conditions listed (Table 1). Equilibrium urea denaturation was observed by monitoring the intrinsic fluorescence of 30 samples equilibrated in urea concentrations ranging from 0 to 8 M using a Perkin-Elmer LS 55 spectrofluorimeter with excitation wavelength at 280 nm and emission at 335 nm. Tris buffer was used rather than the recommended phosphate and HEPES because both bind to the native state of this protein with consequent alteration of its stability and kinetics (Chiti et al., 1998). (FB, FC)
Kinetic Notes mAcP. Maxwell et al 2005. The human protein was expressed and purified as described previously (Taddei et al., 1996). Kinetic unfolding/refolding was followed using a Bio-logic SFM-3 stopped-flow fluorimeter, with excitation at 280 nm and a bandpass filter to monitor emitted fluorescence above 320 nm under conditions listed (Table 1). Equilibrium urea denaturation was observed by monitoring the intrinsic fluorescence of 30 samples equilibrated in urea concentrations ranging from 0 to 8 M using a Perkin-Elmer LS 55 spectrofluorimeter with excitation wavelength at 280 nm and emission at 335 nm. Tris buffer was used rather than the recommended phosphate and HEPES because both bind to the native state of this protein with consequent alteration of its stability and kinetics (Chiti et al., 1998). (FB, FC)
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contact us to make corrections & updates to this data