001     11981
005     20240619091940.0
024 7 _ |2 pmid
|a pmid:19924753
024 7 _ |2 DOI
|a 10.1002/cphc.200900514
024 7 _ |2 WOS
|a WOS:000277666900010
037 _ _ |a PreJuSER-11981
041 _ _ |a eng
082 _ _ |a 540
084 _ _ |2 WoS
|a Chemistry, Physical
084 _ _ |2 WoS
|a Physics, Atomic, Molecular & Chemical
100 1 _ |0 P:(DE-Juel1)VDB2684
|a Monkenbusch, M.
|b 0
|u FZJ
245 _ _ |a Observation of protein domain motions by neutron spectroscopy
260 _ _ |a Weinheim
|b Wiley-VCH Verl.
|c 2010
300 _ _ |a 1187 - 1194
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |0 10582
|a ChemPhysChem
|v 11
|x 1439-4235
|y 6
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a High-resolution inelastic neutron scattering, which is available with neutron spin-echo spectroscopy (NSE) is introduced as a tool for the analysis of biomolecule flexibility. Coherent scattering in a range where it is sensitive to length scales of nanometers and covering a time range from picoseconds to several 100 ns makes the motion of larger subdomains within proteins visible. We show that and how the internal domain motion within a protein in solution can be measured. Comparison with displacement patterns from normal mode analysis provides further insight into the nature of the geometry of the motions that lead to the observed dynamic signature. The NSE experiment on alcohol dehydrogenase (ADH) is used as example to illustrate the general principles of the method.
536 _ _ |0 G:(DE-Juel1)FUEK505
|2 G:(DE-HGF)
|a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
|c P45
|x 0
536 _ _ |0 G:(DE-Juel1)FUEK415
|a Großgeräte für die Forschung mit Photonen, Neutronen und Ionen (PNI)
|c P55
|x 1
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Alcohol Dehydrogenase: chemistry
650 _ 2 |2 MeSH
|a Molecular Dynamics Simulation
650 _ 2 |2 MeSH
|a NAD: chemistry
650 _ 2 |2 MeSH
|a Neutron Diffraction
650 _ 2 |2 MeSH
|a Protein Structure, Tertiary
650 _ 7 |0 53-84-9
|2 NLM Chemicals
|a NAD
650 _ 7 |0 EC 1.1.1.1
|2 NLM Chemicals
|a Alcohol Dehydrogenase
650 _ 7 |2 WoSType
|a J
653 2 0 |2 Author
|a conformation analysis
653 2 0 |2 Author
|a neutron scattering
653 2 0 |2 Author
|a neutron spectroscopy
653 2 0 |2 Author
|a protein domain motions
653 2 0 |2 Author
|a protein structures
700 1 _ |0 P:(DE-Juel1)130917
|a Richter, D.
|b 1
|u FZJ
700 1 _ |0 P:(DE-Juel1)130542
|a Biehl, R.
|b 2
|u FZJ
773 _ _ |0 PERI:(DE-600)2025223-7
|a 10.1002/cphc.200900514
|g Vol. 11, p. 1187 - 1194
|p 1187 - 1194
|q 11<1187 - 1194
|t ChemPhysChem
|v 11
|x 1439-4235
|y 2010
856 7 _ |u http://dx.doi.org/10.1002/cphc.200900514
909 C O |o oai:juser.fz-juelich.de:11981
|p VDB
913 1 _ |0 G:(DE-Juel1)FUEK505
|b Schlüsseltechnologien
|k P45
|l Biologische Informationsverarbeitung
|v BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
|x 0
913 1 _ |0 G:(DE-Juel1)FUEK415
|b Struktur der Materie
|k P55
|l Großgeräteforschung mit Photonen, Neutronen und Ionen
|v Großgeräte für die Forschung mit Photonen, Neutronen und Ionen (PNI)
|x 1
913 2 _ |0 G:(DE-HGF)POF3-623
|1 G:(DE-HGF)POF3-620
|2 G:(DE-HGF)POF3-600
|a DE-HGF
|b Forschungsbereich Materie
|l In-house research on the structure, dynamics and function of matter
|v Neutrons for Research on Condensed Matter
|x 0
914 1 _ |y 2010
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
920 1 _ |0 I:(DE-Juel1)VDB784
|d 31.12.2010
|g IFF
|k IFF-4
|l Streumethoden
|x 1
920 1 _ |0 I:(DE-Juel1)VDB785
|d 31.12.2010
|g IFF
|k IFF-5
|l Neutronenstreuung
|x 0
920 1 _ |0 I:(DE-Juel1)JCNS-20121112
|k Jülich Centre for Neutron Science JCNS (JCNS) ; JCNS
|l JCNS
|x 2
970 _ _ |a VDB:(DE-Juel1)123412
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981 _ _ |a I:(DE-Juel1)JCNS-ILL-20110128


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