Study of protein dynamics in solution by measurement of 13 C α - 13 CO NOE and 13 CO longitudinal relaxation
dc.contributor.author | Zeng, Lei | en_US |
dc.contributor.author | Fischer, Mark W. F. | en_US |
dc.contributor.author | Zuiderweg, Erik R. P. | en_US |
dc.date.accessioned | 2006-09-08T21:00:55Z | |
dc.date.available | 2006-09-08T21:00:55Z | |
dc.date.issued | 1996-03 | en_US |
dc.identifier.citation | Zeng, Lei; Fischer, Mark W. F.; Zuiderweg, Erik R. P.; (1996). "Study of protein dynamics in solution by measurement of 13 C α - 13 CO NOE and 13 CO longitudinal relaxation." Journal of Biomolecular NMR 7(2): 157-162. <http://hdl.handle.net/2027.42/43052> | en_US |
dc.identifier.issn | 0925-2738 | en_US |
dc.identifier.issn | 1573-5001 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/43052 | |
dc.description.abstract | 13 C α - 13 CO homonuclear NOE and 13 CO T 1 relaxation were measured for a 20 kDa protein using tripleresonance pulse sequences. The experiments were sufficiently sensitive to obtain statistically significant differences in relaxation parameters over the molecule. The 13 C α - 13 CO cross-relaxation rate, obtained from these data, is directly proportional to an order parameter describing local motion and it is largely independent of the local correlation time. It is therefore a relatively straightforward observable for the identification of local dynamics. | en_US |
dc.format.extent | 475471 bytes | |
dc.format.extent | 3115 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Kluwer Academic Publishers; ESCOM Science Publishers B.V. ; Springer Science+Business Media | en_US |
dc.subject.other | Chemistry | en_US |
dc.subject.other | Polymer Sciences | en_US |
dc.subject.other | Animal Anatomy / Morphology / Histology | en_US |
dc.subject.other | C α CO NOE | en_US |
dc.subject.other | Triple-resonance NMR | en_US |
dc.subject.other | Longitudinal Relaxation | en_US |
dc.subject.other | Carbonyl NMR | en_US |
dc.subject.other | Order Parameters | en_US |
dc.subject.other | T4-lysozyme | en_US |
dc.title | Study of protein dynamics in solution by measurement of 13 C α - 13 CO NOE and 13 CO longitudinal relaxation | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Natural Resources and Environment | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Biophysics Research Division, The University of Michigan, 930 N. University Avenue, 48109-1055, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationum | Biophysics Research Division, The University of Michigan, 930 N. University Avenue, 48109-1055, Ann Arbor, MI, USA; Department of Physics, The University of Michigan, 930 N. University Avenue, 48109-1055, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationum | Biophysics Research Division, The University of Michigan, 930 N. University Avenue, 48109-1055, Ann Arbor, MI, USA; Department of Biological Chemistry, The University of Michigan, 930 N. University Avenue, 48109-1055, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 22911008 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/43052/1/10858_2004_Article_BF00203826.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1007/BF00203826 | en_US |
dc.identifier.source | Journal of Biomolecular NMR | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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