The DOI matches its Crossref record; 57 of the 57 references it cites were found in a registry or an index.
Nuclear Magnetic Resonance Studies of Biopolymer Dynamics
Abstract
NMR spectroscopy is a powerful approach for quantitating molecular conformational dynamics at multiple atomic sites and over multiple time scales. Extensive studies by solution and solid-state NMR spectroscopy of spin relaxation and line shapes in biological macromolecules have been performed in order to characterize the amplitudes, time scales, and energetics of intramolecular conformational modes and to elucidate the relationships between conformational dynamics, structure, and function. This review describes NMR spectroscopic methods for investigation of conformational dynamics together with theoretical descriptions appropriate for interpretation and simulation of the techniques, surveys the range of results available from solution and solid state NMR studies of proteins and other biomolecules, and identifies opportunities for further individual and collaborative development of solution and solid state NMR techniques for characterizing the dynamical properties of biological macromolecules.
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Cites
Modified Spin-Echo Method for Measuring Nuclear Relaxation Times
Meiboom, S., & Gill, D. (1958) · Review of Scientific Instruments · doi:10.1063/1.1716296 · Cited by 6,022
Lipari, G., & Szabo, A. (1982) · Journal of the American Chemical Society · doi:10.1021/ja00381a009 · Cited by 3,777
Farrow, N. A., Muhandiram, R., Singer, A. U., Pascal, S. M., Kay, C. M., Gish, G., Shoelson, S. E., Pawson, T., Forman-Kay, J. D., & Kay, L. E. (1994) · Biochemistry · doi:10.1021/bi00185a040 · Cited by 2,091
Enhancement of nuclear magnetic resonance signals by polarization transfer
Morris, G. A., & Freeman, R. (1979) · Journal of the American Chemical Society · doi:10.1021/ja00497a058 · Cited by 2,015
Lipari, G., & Szabo, A. (1982) · Journal of the American Chemical Society · doi:10.1021/ja00381a010 · Cited by 1,837
Deuterium magnetic resonance: theory and application to lipid membranes
Seelig, J. (1977) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500002948 · Cited by 1,284
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Conformational Substates in Proteins
Frauenfelder, H., Parak, F., & Young, R. D. (1988) · Annual Review of Biophysics and Biophysical Chemistry · doi:10.1146/annurev.bb.17.060188.002315 · Cited by 993
Backbone Dynamics of Ribonuclease HI: Correlations with Structure and Function in an Active Enzyme
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Hhal methyltransferase flips its target base out of the DNA helix
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Cited by
Palmer, A. G., Kroenke, C. D., & Patrick Loria, J. (2001) · Methods in Enzymology · doi:10.1016/s0076-6879(01)39315-1 · Cited by 938
Self-citationGarcı́a de la Torre, J., Huertas, M. L., & Carrasco, B. (2000) · Journal of Magnetic Resonance · doi:10.1006/jmre.2000.2170 · Cited by 551
Investigation of Molecular Motions by Lee-Goldburg Cross-Polarization NMR Spectroscopy
Hong, M., Yao, X., Jakes, K., & Huster, D. (2002) · The Journal of Physical Chemistry B · doi:10.1021/jp0156064 · Cited by 137
Metadata
- Authors
- Palmer, A. G., Williams, J., & McDermott, A.
- Venue
- The Journal of Physical Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1996-01-01
- Volume
- 100
- Issue
- 31
- Pages
- 13293-13310
- ISSN
- 0022-3654 (ISSN-L)
- 1541-5740
- OpenAlex
- W2092985709
- Cited by
- 294
- References
- 57
- FWCI
- 9.21
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
