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ID: 16495.0, MPI für biophysikalische Chemie / NMR-basierte Strukturbiologie (Prof. Christian Griesinger)
Evaluation of uncertainty in alignment tensors obtained from dipolar couplings
Authors:Zweckstetter, M.; Bax, A.
Language:English
Date of Publication (YYYY-MM-DD):2002-06
Title of Journal:Journal of Biomolecular NMR
Volume:23
Issue / Number:2
Start Page:127
End Page:137
Review Status:Peer-review
Audience:Not Specified
Abstract / Description:Residual dipolar couplings and their corresponding alignment tensors are useful for structural analysis of macromolecules. The error in an alignment tensor, derived from residual dipolar couplings on the basis of a known structure, is determined not only by the accuracy of the measured couplings but also by the uncertainty in the structure (structural noise). This dependence is evaluated quantitatively on the basis of simulated structures using Monte-Carlo type analyses. When large numbers of dipolar couplings are available, structural noise is found to result in a systematic underestimate of the magnitude of the alignment tensor. Particularly in cases where only few dipolar couplings are available, structural noise can cause significant errors in best-fitted alignment tensor values, making determination of the relative orientation of small fragments and evaluation of local backbone mobility from dipolar couplings difficult. An example for the protein ubiquitin demonstrates the inherent limitations in characterizing motions on the basis of local alignment tensor magnitudes.
Free Keywords:alignment tensor; backbone dynamics; dipolar coupling; error analysis; liquid crystal; order matrix; protein structure determination; ubiquitin
Comment of the Author/Creator:Date: 2002, JUN
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für biophysikalische Chemie/AG Markus Zweckstetter
External Affiliations:NIDDKD, Chem Phys Lab, NIH, Bldg 2, Bethesda, MD 20892 USA;
Identifiers:URL:http://springerlink.metapress.com/content/ptb0r768...
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