Protein Folding Database: Measurement Report

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

Compare Data

compare with other measurements for proteins in this SCOP Family (4)

Protein Data
Protein Name	Actin binding protein 1 SH3 domain (Abp1 SH3)
Oligomeric State	Monomer
Folding Mechanism	Not characterised
Intermediates	0
Phi Pattern	No phi value analysis
SCOP Class	Beta \| goto SCOP
SCOP Family	SH3 domain \| goto SCOP

Construct Data
Species	Common Yeast (Saccharomyces cerevisiae)	goto 3D view
Sequence	MAPWATAEYDYDAAEDNELTFVENDKIINIEFVDDDWWLGELEKDGSKGL FPSNYVSLGNLEHHHHHH Blast PFD \| Blast NCBI NR
Length	69
Molecular Weight	7909.52Da
Fusion	C-terminal hexahistidine
PDB ID	1JO8 \| goto PDB
PDB Resolution	1.3Å
Chain	A
Residues	1 - 58
SCOP ID	74921 \| goto SCOP
UniProt ID	ABP1_YEAST \| goto UniProt
Relative Contact Order	16.23

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

Graphical Analysis Data

Chevron Plot

unfolding & refolding data

ln(k_uH₂O) (s^-1)	ln(k_fH₂O) (s^-1)	m_‡-N (kJ mol^-1 M^-1)	m_‡-D (kJ mol^-1 M^-1)
-2.72 ± 0.08	2.46 ± 0.06	0.83 ± 0.04	-6.36 ± 0.17

Notes on Chevron Plot Calculating

Contact Order Plot Data

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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

Equilibrium Data & Methods

Equilibrium Data

[Denaturant] Minimum (M)	[Denaturant] 50% (M)	m_D-N (m) (kJ mol^-1 M^-1)	∆G_D-N (m) (kJ mol^-1)
ND	ND	-6.9 ± 0.3	13 ± 0.8

Probe

Trp Fluorescence what is this?

Pertubation

Denaturant what is this?

Technique

GdnHCl

Instrument

Aviv ATF 105 Spectrofluorometer

Temperature

298K

Buffer

0.05M Phosphate

Additive 1:

0.1M NaCl

Protein Concentration

Kinetic Data & Methods

Kinetic Unfolding Data

[Denaturant] Minimum (M)	[Denaturant] Maximum (M)	k_u (s^-1)	lnk_u (s^-1)	m_u (M^-1)	m_‡-N (kJ mol^-1 M^-1)
3.5	7	0.06588 ± 0.00021 (0M)	-2.72 ± 0.08 (0M)	ND	0.83 ± 0.04

Kinetic Folding Data

[Denaturant] Minimum (M)	[Denaturant] Maximum (M)	k_fH₂O (s^-1)	ln(k_fH₂O) (s^-1)	m_f (M^-1)	m_‡-D (kJ mol^-1 M^-1)
0.5	2	11.7 ± 0.02	2.46 ± 0.06	ND	-6.36 ± 0.17