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| Hauptseite > Publikationsdatenbank > Structural constraints for the Crh protein from solid-state NMR experiments > print |
| Hauptseite > Publikationsdatenbank > Structural constraints for the Crh protein from solid-state NMR experiments > print |
| 001 | 275 | ||
| 005 | 20200402205331.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:18320329 |
| 024 | 7 | _ | |2 pmc |a pmc:PMC2579321 |
| 024 | 7 | _ | |2 DOI |a 10.1007/s10858-008-9229-3 |
| 024 | 7 | _ | |2 WOS |a WOS:000254804800002 |
| 037 | _ | _ | |a PreJuSER-275 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 084 | _ | _ | |2 WoS |a Biochemistry & Molecular Biology |
| 084 | _ | _ | |2 WoS |a Spectroscopy |
| 100 | 1 | _ | |a Gardiennet, C. |b 0 |0 P:(DE-HGF)0 |
| 245 | _ | _ | |a Structural constraints for the Crh protein from solid-state NMR experiments |
| 260 | _ | _ | |a Dordrecht [u.a.] |b Springer Science + Business Media B.V |c 2008 |
| 300 | _ | _ | |a 239 - 250 |
| 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 | |a Journal of Biomolecular NMR |x 0925-2738 |0 9165 |y 4 |v 40 |
| 500 | _ | _ | |a Record converted from VDB: 12.11.2012 |
| 520 | _ | _ | |a We demonstrate that short, medium and long-range constraints can be extracted from proton mediated, rare-spin detected correlation solid-state NMR experiments for the microcrystalline 10.4 x 2 kDa dimeric model protein Crh. Magnetization build-up curves from cross signals in NHHC and CHHC spectra deliver detailed information on side chain conformers and secondary structure for interactions between spin pairs. A large number of medium and long-range correlations can be observed in the spectra, and an analysis of the resolved signals reveals that the constraints cover the entire sequence, also including inter-monomer contacts between the two molecules forming the domain-swapped Crh dimer. Dynamic behavior is shown to have an impact on cross signals intensities, as indicated for mobile residues or regions by contacts predicted from the crystal structure, but absent in the spectra. Our work validates strategies involving proton distance measurements for large and complex proteins as the Crh dimer, and confirms the magnetization transfer properties previously described for small molecules in solid protein samples. |
| 536 | _ | _ | |a Funktion und Dysfunktion des Nervensystems |c P33 |2 G:(DE-HGF) |0 G:(DE-Juel1)FUEK409 |x 0 |
| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Bacterial Proteins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Dimerization |
| 650 | _ | 2 | |2 MeSH |a Models, Molecular |
| 650 | _ | 2 | |2 MeSH |a Nuclear Magnetic Resonance, Biomolecular: methods |
| 650 | _ | 2 | |2 MeSH |a Phosphoproteins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Protein Conformation |
| 650 | _ | 2 | |2 MeSH |a Protons |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Bacterial Proteins |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Crh protein, Bacillus subtilis |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Phosphoproteins |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Protons |
| 650 | _ | 7 | |a J |2 WoSType |
| 653 | 2 | 0 | |2 Author |a catabolite repression histidine-containing phosphocarrier protein (Crh) |
| 653 | 2 | 0 | |2 Author |a distance constraints |
| 653 | 2 | 0 | |2 Author |a MAS |
| 653 | 2 | 0 | |2 Author |a 3D protein structure |
| 653 | 2 | 0 | |2 Author |a solid-state NMR spectroscopy |
| 700 | 1 | _ | |a Loquet, A. |b 1 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Bockmann, A |b 2 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Etzkorn, M. |b 3 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Heise, H. |b 4 |u FZJ |0 P:(DE-Juel1)VDB77857 |
| 700 | 1 | _ | |a Baldus, M. |b 5 |0 P:(DE-HGF)0 |
| 773 | _ | _ | |a 10.1007/s10858-008-9229-3 |g Vol. 40, p. 239 - 250 |p 239 - 250 |q 40<239 - 250 |0 PERI:(DE-600)2006645-4 |t Journal of biomolecular NMR |v 40 |y 2008 |x 0925-2738 |
| 856 | 7 | _ | |2 Pubmed Central |u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2579321 |
| 909 | C | O | |o oai:juser.fz-juelich.de:275 |p VDB |
| 913 | 1 | _ | |k P33 |v Funktion und Dysfunktion des Nervensystems |l Funktion und Dysfunktion des Nervensystems |b Gesundheit |0 G:(DE-Juel1)FUEK409 |x 0 |
| 914 | 1 | _ | |y 2008 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
| 920 | 1 | _ | |k INB-2 |l Molekulare Biophysik |d 31.12.2008 |g INB |0 I:(DE-Juel1)VDB805 |x 0 |
| 970 | _ | _ | |a VDB:(DE-Juel1)100531 |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a ConvertedRecord |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a I:(DE-Juel1)ISB-2-20090406 |
| 980 | _ | _ | |a UNRESTRICTED |
| 980 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
| 981 | _ | _ | |a I:(DE-Juel1)IBI-7-20200312 |
| 981 | _ | _ | |a I:(DE-Juel1)ISB-2-20090406 |
| 981 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
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