Toward unified and consistent views of protein dynamics
- PMID: 8075314
- PMCID: PMC1275899
- DOI: 10.1016/S0006-3495(94)80969-5
Toward unified and consistent views of protein dynamics
Comment on
-
13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-Trp variants of Escherichia coli thioredoxin.Biophys J. 1994 Jun;66(6):2111-26. doi: 10.1016/S0006-3495(94)81006-9. Biophys J. 1994. PMID: 8075345 Free PMC article.
Similar articles
-
Conformational analysis of cholecystokinin fragments CCK4, CCK5, and CCK6 by 1H-NMR spectroscopy and fluorescence-transfer measurements.Biopolymers. 1985 Sep;24(9):1663-81. doi: 10.1002/bip.360240903. Biopolymers. 1985. PMID: 4052579 No abstract available.
-
Applications of nuclear magnetic resonance, circular dichroism and fluorescence spectroscopy to the characterization of biological products.Biologicals. 1993 Jun;21(2):119-24. doi: 10.1006/biol.1993.1060. Biologicals. 1993. PMID: 8297591 Review. No abstract available.
-
[Characterization of dynamic behavior of side groups of globular proteins by spin-label, NMR and luminescence polarization methods].Mol Biol (Mosk). 1983 May-Jun;17(3):519-31. Mol Biol (Mosk). 1983. PMID: 6308417 Russian.
-
Kurt Wüthrich, the ETH Zürich, and the development of NMR spectroscopy for the investigation of structure, dynamics, and folding of proteins.Chembiochem. 2003 Mar 3;4(2-3):135-42. doi: 10.1002/cbic.200390023. Chembiochem. 2003. PMID: 12616625 Review. No abstract available.
-
Protein dynamics from NMR.Nat Struct Biol. 1998 Jul;5 Suppl:513-7. doi: 10.1038/755. Nat Struct Biol. 1998. PMID: 9665181 Review.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources