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

Expand   Protein Data
Protein Name Apo-azurin (Apo-azurin)
Oligomeric State Monomer
Folding Mechanism Not characterised
Intermediates 0
Phi Pattern No phi value analysis
SCOP Class Beta   |   goto SCOP
SCOP Family Plastocyanin/azurin-like   |   goto SCOP

Expand   Construct Data
Species Pseudomonas
aeruginosa (Pseudomonas aeruginosa)

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Sequence AECSVDIQGNDQMQFNTNAITVDKSCKQFTVNLSHPGNLPKNVMGHNWVL
STAADMQGVVTDGMASGLDKDYLKPDDSRVIAHTKLIGSGEKDSVTFDVS
KLKEGEQYMFFCTFPGHSALMKGTLTLK

Blast PFD  |  Blast NCBI NR
Length 129
Molecular Weight 13927.8Da
Fusion None
PDB ID 1E65   |   goto PDB  
PDB Resolution 1.85Å
Chain Any chain
Residues 1 - 128
SCOP ID 49533   |   goto SCOP
UniProt ID AZUR_PSEAE   |   goto UniProt
Relative Contact Order 16.05

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 8
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)
-4.02 ± 0.23 4.91 ± 0.09 5.06 ± 0.19 -8.03 ± 0.23
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 -17.6 ± 0.9 29.2 ± 1.5
Probe Trp Fluorescence  what is this?
Pertubation Denaturant  what is this?
Technique GdnHCl
Instrument Varian Eclipse Fluorescence Spectrophotometer
Temperature 298K
pH 7
Buffer 0.0050M Acetate
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)
2 3.5 0.01795 ± 0.00048 (0M) -4.02 ± 0.23 (0M) ND 5.06 ± 0.19
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)
0.42 1.6 135.64 ± 0.55 4.91 ± 0.09 ND -8.03 ± 0.23
Probe Trp Fluorescence  what is this?
Pertubation Denaturant  what is this?
Technique GdnHCl
Instrument Applied Photophysics DX.18MV Sequential Mixing Stopped-flow Spectrometer
Temperature 298K
pH 7
Buffer 0.0050M Acetate
Protein Concentration 0.01M
Unfolding Fit Linear
Refolding Fit Linear

Expand   Notes & Comments on this measurement
Measurement Notes
Protein Notes sandwich; 7 strands in 2 sheets, greek-key.
Construct Notes
Equilibrium Notes GuHCl-induced equilibrium unfolding of apo-azurin was monitored by tryotophan fluorescence (Varian Eclipse; excitation 285 nm, emission 308 nm, 5 nm band-pass). There was no protein-concentration dependence for the unfolding transition (in the range 5-100 microM). The reaction was fully reversible.
Kinetic Notes Time-resolved folding measurements were made on an Applied Photophysics DX.18MV stopped-flow reaction analyzer (with two monochromators) in its fluorescence (excitation at 285 nm; emission at 308 nm; 8 nm band-pass, 0.2 cm path) mode. For each experimental condition, 5-8 transients were averaged. Refolding and unfolding of apo-azurin were monitored by tryptophan fluorescence. For unfolding, five parts of denaturant solution were mixed with 1 part of protein solution (10 µM final protein concentration). Refolding was initiated from 2.5 M GuHCl by 1:5 mixing with buffer solutions including appropriate GuHCl concentrations. No missing amplitude was observed within the instrument dead time (6-8 ms for 1:5 mixing).
Comments view comments on this measurement

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