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  The quest for simplicity: Remarks on the free-approach models.

Jaremko, L., Jaremko, M., Nowakowski, M., & Ejchart, A. (2015). The quest for simplicity: Remarks on the free-approach models. Journal of Physical Chemistry B, 119(36), 11978-11987. doi:10.1021/acs.jpcb.5b07181.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-6541-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-6003-B
Genre: Journal Article

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Jaremko, L.1, Author              
Jaremko, M.1, Author              
Nowakowski, M., Author
Ejchart, A., Author
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1Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_578567              

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 Abstract: Nuclear magnetic relaxation provides a powerful method giving insight into molecular motions at atomic resolution on a broad time scale. Dynamics of biological macromolecules has been widely exploited by measuring 15N and 13C relaxation data. Interpretation of these data relies almost exclusively on the use of the model-free approach (MFA) and its extended version (EMFA) which requires no particular physical model of motion and a small number of parameters. It is shown that EMFA is often unable to cope with three different time scales and fails to describe slow internal motions properly. In contrast to EMFA, genuine MFA with two time scales can reproduce internal motions slower than the overall tumbling. It is also shown that MFA and simplified EMFA are equivalent with respect to the values of the N–H bond length and chemical shift anisotropy. Therefore, the vast majority of 15N relaxation data for proteins can be satisfactorily interpreted solely with MFA.

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Language(s): eng - English
 Dates: 2015-08-282015-09-10
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1021/acs.jpcb.5b07181
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Title: Journal of Physical Chemistry B
Source Genre: Journal
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Pages: - Volume / Issue: 119 (36) Sequence Number: - Start / End Page: 11978 - 11987 Identifier: -