SASDDF6: Myelin basic protein

Basic information

• Entry: Database: SASBDB / ID: SASDDF6

Sample

Myelin basic protein

• Myelin basic protein (protein), Bos taurus

Function / homology

Function:

compact myelin / structural constituent of myelin sheath / internode region of axon / myelination / cell periphery / phospholipid binding / myelin sheath / calmodulin binding / neuronal cell body / protein-containing complex / plasma membrane

Domain/homology:

Myelin basic protein / Myelin basic protein / Myelin basic protein signature.

Component:

Myelin basic protein

• Biological species: Bos taurus (cattle)
• Citation: Journal: J Am Chem Soc / Year: 2014; Title: Internal nanosecond dynamics in the intrinsically disordered myelin basic protein.; Authors: Andreas M Stadler / Laura Stingaciu / Aurel Radulescu / Olaf Holderer / Michael Monkenbusch / Ralf Biehl / Dieter Richter / ; Abstract: Intrinsically disordered proteins lack a well-defined folded structure and contain a high degree of structural freedom and conformational flexibility, which is expected to enhance binding to their physiological targets. In solution and in the lipid-free state, myelin basic protein belongs to that class of proteins. Using small-angle scattering, the protein was found to be structurally disordered similar to Gaussian chains. The combination of structural and hydrodynamic information revealed an intermediary compactness of the protein between globular proteins and random coil polymers. Modeling by a coarse-grained structural ensemble gave indications for a compact core with flexible ends. Neutron spin-echo spectroscopy measurements revealed a large contribution of internal dynamics to the overall diffusion. The experimental results showed a high flexibility of the structural ensemble. Displacement patterns along the first two normal modes demonstrated that collective stretching and bending motions dominate the internal modes. The observed dynamics represent nanosecond conformational fluctuations within the reconstructed coarse-grained structural ensemble, allowing the exploration of a large configurational space. In an alternative approach, we investigated if models from polymer theory, recently used for the interpretation of fluorescence spectroscopy experiments on disordered proteins, are suitable for the interpretation of the observed motions. Within the framework of the Zimm model with internal friction (ZIF), a large offset of 81.6 ns is needed as an addition to all relaxation times due to intrachain friction sources. The ZIF model, however, shows small but systematic deviations from the measured data. The large value of the internal friction leads to the breakdown of the Zimm model.

Contact author

• Andreas Stadler (Forschungszentrum Jülich)

Models

• Model #1987: ; Type: mix / Radius of dummy atoms: 1.90 A / Chi-square value: 0.908209 / P-value: 0.000947; Search similar-shape structures of this assembly by Omokage search (details)
• Model #1988: ; Type: mix / Radius of dummy atoms: 1.90 A / Chi-square value: 0.908209 / P-value: 0.000947; Search similar-shape structures of this assembly by Omokage search (details)
• Model #1989: ; Type: mix / Radius of dummy atoms: 1.90 A / Chi-square value: 0.908209 / P-value: 0.000947; Search similar-shape structures of this assembly by Omokage search (details)
• Model #1990: ; Type: mix / Radius of dummy atoms: 1.90 A / Chi-square value: 0.908209 / P-value: 0.000947; Search similar-shape structures of this assembly by Omokage search (details)
• Model #1991: ; Type: mix / Radius of dummy atoms: 1.90 A / Chi-square value: 0.908209 / P-value: 0.000947; Search similar-shape structures of this assembly by Omokage search (details)
• Model #1992: ; Type: mix / Radius of dummy atoms: 1.90 A / Chi-square value: 0.908209 / P-value: 0.000947; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: Myelin basic protein / Specimen concentration: 4.5 mg/ml
• Buffer: Name: 20 mM NaH2PO4/ Na2HPO4, 99.9% D2O / pH: 4.8 / Comment: deuterium oxide

Entity #1062

Type: protein / Description: Myelin basic protein / Formula weight: 18.323 / Num. of mol.: 1 / Source: Bos taurus / References: UniProt: P02687
Sequence:

AAQKRPSQRS KYLASASTMD HARHGFLPRH RDTGILDSLG RFFGSDRGAP KRGSGKDGHH AARTTHYGSL PQKAQGHRPQ DENPVVHFFK NIVTPRTPPP SQGKGRGLSL SRFSWGAEGQ KPGFGYGGRA SDYKSAHKGL KGHDAQGTLS KIFKLGGRDS RSGSPMARR

Experimental information

• Beam: Instrument name: ESRF BM29 / City: Grenoble / 国: France / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.099 Å
• Detector: Name: Pilatus 1M / Type: Dectris / Pixsize x: 172 mm

Scan

Title: Myelin basic protein / Measurement date: Feb 21, 2013 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 2 sec. / Number of frames: 10 / Unit: 1/nm /

	Min	Max
Q	0.1367	4.525

Distance distribution function P(R)

Sofotware P(R): GNOM 5.0 / Number of points: 520 /

	Min	Max
Q	0.167111	2.41986
P(R) point	1	520
R	0	11.06

Result

Type of curve: single_conc /

	Experimental	Standard	Standard error
MW	20.49 kDa	20.49 kDa	0.01

	P(R)	Guinier	Guinier error
Forward scattering, I0	20.72	20.49	0.023
Radius of gyration, Rg	3.461 nm	3.3 nm	0.01

	Min	Max
D	-	11.06
Guinier point	8	60