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|a 10.1039/c0sm00683a
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041 _ _ |a eng
082 _ _ |a 530
084 _ _ |2 WoS
|a Chemistry, Physical
084 _ _ |2 WoS
|a Materials Science, Multidisciplinary
084 _ _ |2 WoS
|a Physics, Multidisciplinary
084 _ _ |2 WoS
|a Polymer Science
100 1 _ |0 P:(DE-Juel1)130542
|a Biehl, R.
|b 0
|u FZJ
245 _ _ |a Exploring internal protein dynamics by neutron spin echo spectroscopy
260 _ _ |a Cambridge
|b Royal Society of Chemistry (RSC)
|c 2011
300 _ _ |a 1299 - 1307
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|a Soft Matter
|v 7
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500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a 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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|a Forschungs-Neutronenquelle Heinz Maier-Leibnitz
|e J-NSE: Neutron spin-echo spectrometer
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700 1 _ |0 P:(DE-Juel1)VDB2684
|a Monkenbusch, M.
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700 1 _ |0 P:(DE-Juel1)130917
|a Richter, D.
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|g Vol. 7, p. 1299 - 1307
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|t Soft matter
|v 7
|x 1744-683X
|y 2011
856 7 _ |u http://dx.doi.org/10.1039/c0sm00683a
856 4 _ |u https://juser.fz-juelich.de/record/11985/files/FZJ-11985.pdf
|y Published under German "Allianz" Licensing conditions on 2010-11-15. Available in OpenAccess from 2011-11-15
|z Published final document.
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