| Home > Publications database > Observation of protein domain motions by neutron spectroscopy > print |
| 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 |
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| 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. |
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| 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 |
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| 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 |
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| 914 | 1 | _ | |y 2010 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
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