The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Probing molecular motion by NMR
Open accessAbstract
Recently developed solution NMR methods for measuring 2H, 13C, and 15N spin relaxation, coupled with biosynthetic isotopic enrichment, permit the characterization of backbone and sidechain dynamical properties of proteins on picosecond/nanosecond and microsecond/millisecond timescales. Theoretical interpretations of the relaxation data provide insights into the biophysical and functional properties of proteins.
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Cites
Lipari, G., & Szabo, A. (1982) · Journal of the American Chemical Society · doi:10.1021/ja00381a009 · Cited by 3,777
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-citationTwo-State Allosteric Behavior in a Single-Domain Signaling Protein
Volkman, B. F., Lipson, D., Wemmer, D. E., & Kern, D. (2001) · Science · doi:10.1126/science.291.5512.2429 · Cited by 593
An NMR Perspective on Enzyme Dynamics
Boehr, D. D., Dyson, H. J., & Wright, P. E. (2006) · Chemical Reviews · doi:10.1021/cr050312q · Cited by 458
Vass, E., Hollósi, M., Besson, F., & Buchet, R. (2003) · Chemical Reviews · doi:10.1021/cr000100n · Cited by 288
Stumber, M., Geyer, M., Graf, R., Robert Kalbitzer, H., Scheffzek, K., & Haeberlen, U. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01010-0 · Cited by 22
Metadata
- Authors
- Palmer, A. G.
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 1997-10
- Volume
- 7
- Issue
- 5
- Pages
- 732-737
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W2131823126
- Cited by
- 242
- References
- 1
- FWCI
- 1.43
- Type
- journal article
- Language
- en
- Open access
- hybrid
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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.