The Quest for Simplicity: Remarks on the Free-Approach Models
| Autor: | Michał Nowakowski, Łukasz Jaremko, Andrzej Ejchart, Mariusz Jaremko |
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| Rok vydání: | 2015 |
| Předmět: |
Nuclear magnetic relaxation
Magnetic Resonance Spectroscopy Scale (ratio) Chemistry media_common.quotation_subject Small number Statistics as Topic Proteins Models Theoretical Surfaces Coatings and Films Theoretical physics Atomic resolution chemistry [Proteins] Materials Chemistry Molecular motion ddc:530 Statistical physics Simplicity Relaxation (approximation) Physical and Theoretical Chemistry Anisotropy media_common |
| Zdroj: | The journal of physical chemistry Journal of Physical Chemistry B |
| ISSN: | 1520-5207 1520-6106 |
| DOI: | 10.1021/acs.jpcb.5b07181 |
| Popis: | 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 (15)N and (13)C 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 (15)N relaxation data for proteins can be satisfactorily interpreted solely with MFA. |
| Databáze: | OpenAIRE |
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