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Theory, Practice, and Applications of Paramagnetic Relaxation Enhancement for the Characterization of Transient Low-Population States of Biological Macromolecules and Their Complexes
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ADVERTISEMENT RETURN TO ISSUEPREVReviewNEXTTheory, Practice, and Applications of Paramagnetic Relaxation Enhancement for the Characterization of Transient Low-Population States of Biological Macromolecules and Their ComplexesG. Marius Clore*† and Junji Iwahara*‡View Author Information Laboratory of Chemical Physics, Building 5, National Institute of Diabetes and Digestive and Kidney Disease, National Institutes of Health, Bethesda, Maryland 20892-0520, and Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, Texas 77555-0647* E-mail: G.M.C., [email protected]; J.I., [email protected]†National Institutes of Health.‡University of Texas Medical Branch.Cite this: Chem. Rev. 2009, 109, 9, 4108–4139Publication Date (Web):June 12, 2009Publication History Received26 January 2009Published online12 June 2009Published inissue 9 September 2009https://pubs.acs.org/doi/10.1021/cr900033phttps://doi.org/10.1021/cr900033preview-articleACS PublicationsCopyright © 2009 American Chemical SocietyRequest reuse permissionsArticle Views10379Altmetric-Citations637LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose SUBJECTS:Crystal structure,Genetics,Macromolecules,Peptides and proteins,Solvents Get e-Alerts
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Cites
NMR with Proteins and Nucleic Acids
Wüthrich, K. (1986) · Europhysics News · doi:10.1051/epn/19861701011 · Cited by 7,989
Intrinsically unstructured proteins and their functions
Dyson, H. J., & Wright, P. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1589 · Cited by 3,871
Lipari, G., & Szabo, A. (1982) · Journal of the American Chemical Society · doi:10.1021/ja00381a009 · Cited by 3,777
Relaxation Processes in a System of Two Spins
Solomon, I. (1955) · Physical Review · doi:10.1103/physrev.99.559 · Cited by 3,278
Funnels, pathways, and the energy landscape of protein folding: A synthesis
Bryngelson, J. D., Onuchic, J. N., Socci, N. D., & Wolynes, P. G. (1995) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340210302 · Cited by 2,648
Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules
Lipari, G. (1982) · Journal of the American Chemical Society · Cited by 2,525
The Xplor-NIH NMR molecular structure determination package
Schwieters, C. D., Kuszewski, J. J., Tjandra, N., & Marius Clore, G. (2003) · Journal of Magnetic Resonance · doi:10.1016/s1090-7807(02)00014-9 · Cited by 2,369
THEORY OF PROTEIN FOLDING: The Energy Landscape Perspective
Onuchic, J. N., Luthey-Schulten, Z., & Wolynes, P. G. (1997) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.48.1.545 · Cited by 2,210
Tjandra, N., & Bax, A. (1997) · Science · doi:10.1126/science.278.5340.1111 · Cited by 1,719
Structural chemistry and molecular biology
Rich, A., Davidson, N., & Pauling, L. C. (1968) · Medical Entomology and Zoology · Cited by 1,702
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Metadata
- Authors
- Clore, G. M., & Iwahara, J.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2009-06-12
- Volume
- 109
- Issue
- 9
- Pages
- 4108-4139
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W2009881858
- Cited by
- 782
- References
- 173
- FWCI
- 1.90
- Type
- journal article
- Language
- en
- Open access
- green
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