The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Methyl Groups as Probes of Structure and Dynamics in NMR Studies of High‐Molecular‐Weight Proteins
Abstract
Solution NMR studies of biomolecules are typically limited by the molecules' molecular weight. Here we report strategies based on the use of highly deuterated, methyl‐protonated proteins that facilitate both structural and motional studies of molecules on the order of 100 kDa. Approaches and concepts are illustrated with applications to the enzyme malate synthase G, a monomeric 723‐residue protein.
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Cites
Protein backbone angle restraints from searching a database for chemical shift and sequence homology
Cornilescu, G., Delaglio, F., & Bax, A. (1999) · Journal of Biomolecular NMR · doi:10.1023/a:1008392405740 · Cited by 2,957
The glyoxylate cycle is required for fungal virulence
Lorenz, M. C., & Fink, G. R. (2001) · Nature · doi:10.1038/35083594 · Cited by 745
Cited by
Tugarinov, V., Kanelis, V., & Kay, L. E. (2006) · Nature Protocols · doi:10.1038/nprot.2006.101 · Cited by 537
Self-citationIgumenova, T. I., Frederick, K. K., & Wand, A. J. (2006) · Chemical Reviews · doi:10.1021/cr040422h · Cited by 314
Metadata
- Authors
- Tugarinov, V., & Kay, L. E.
- Venue
- ChemBioChem
- Publisher
- Wiley
- Published
- 2005-09
- Volume
- 6
- Issue
- 9
- Pages
- 1567-1577
- ISSN
- 1439-4227 (ISSN-L)
- 1439-7633
- OpenAlex
- W1983099248
- Cited by
- 198
- References
- 2
- FWCI
- 4.19
- Type
- journal article
- Language
- en
- Open access
- closed
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- Tugarinov, V., & Kay, L. E. (2005). Methyl Groups as Probes of Structure and Dynamics in NMR Studies of High‐Molecular‐Weight Proteins. ChemBioChem. https://doi.org/10.1002/cbic.200500110
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