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Cited by 344

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

NMR Probes of Molecular Dynamics: Overview and Comparison with Other Techniques

Palmer III, Arthur G.·2001·Annual Review of Biophysics and Biomolecular Structure

Abstract

▪ Abstract NMR spin relaxation spectroscopy is a powerful approach for characterizing intramolecular and overall rotational motions in proteins. This review describes experimental methods for measuring laboratory frame spin relaxation rate constants by high-resolution solution-state NMR spectroscopy, together with theoretical approaches for interpreting spin relaxation data in order to quantify protein conformational dynamics on picosecond-nanosecond time scales. Recent applications of these techniques to proteins are surveyed, and investigations of the contribution of conformational chain entropy to protein function are highlighted. Insights into the dynamical properties of proteins obtained from NMR spin relaxation spectroscopy are compared with results derived from other experimental and theoretical techniques.

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Metadata

Authors
Palmer III, A. G.
Venue
Annual Review of Biophysics and Biomolecular Structure
Published
2001-06
Volume
30
Issue
1
Pages
129-155
ISSN
  • 1056-8700 (ISSN-L)
  • 1545-4266
OpenAlex
W2115549726
Cited by
344
References
2
FWCI
6.30
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: NMR Probes of Molecular Dynamics: Overview and Comparison with Other Techniques. https://app.cochat.ai/papers/10.1146/annurev.biophys.30.1.129
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Palmer III, A. G. (2001). NMR Probes of Molecular Dynamics: Overview and Comparison with Other Techniques. Annual Review of Biophysics and Biomolecular Structure. https://doi.org/10.1146/annurev.biophys.30.1.129

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.