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This title appears in the Scientific Report : 2012 

Exploring internal protein dynamics by neutron spin echo spectroscopy

Exploring internal protein dynamics by neutron spin echo spectroscopy

The activity of proteins is often related to configuration changes that concern single atoms or amino acids or entire subdomains within the protein. The corresponding length and timescale reach from sub-Angstrom and picoseconds to nanometers and several tens of nanoseconds and beyond. We focus here...

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Personal Name(s): Biehl, R.
Monkenbusch, M. / Richter, D.
Contributing Institute: Neutronenstreuung; ICS-1
JCNS; JCNS
Published in: Soft matter, 7 (2011) S. 1299 - 1307
Imprint: Cambridge Royal Society of Chemistry (RSC) 2011
Physical Description: 1299 - 1307
DOI: 10.1039/c0sm00683a
Document Type: Journal Article
Research Program: Großgeräte für die Forschung mit Photonen, Neutronen und Ionen (PNI)
BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
Series Title: Soft Matter 7
Subject (ZB):
J
Link: Get full text
Published under German "Allianz" Licensing conditions on 2010-11-15. Available in OpenAccess from 2011-11-15
Publikationsportal JuSER
Please use the identifier: http://dx.doi.org/10.1039/c0sm00683a in citations.
Please use the identifier: http://hdl.handle.net/2128/7257 in citations.

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The activity of proteins is often related to configuration changes that concern single atoms or amino acids or entire subdomains within the protein. The corresponding length and timescale reach from sub-Angstrom and picoseconds to nanometers and several tens of nanoseconds and beyond. We focus here on the slow motions on several ten nanosecond timescales of complete domains and show that and how these can be accessed by means of small angle neutron scattering and neutron spin-echo spectroscopy. In particular neutron spin echo spectroscopy is able to access timescales up to several hundred nanoseconds. Further insight into domain dynamics can be achieved by modelling the dynamics in comparison with the experimental data.

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