Isotope labeling strategies for the study of high-molecular-weight proteins by solution NMR spectroscopy
By V. Tugarinov, V. Kanelis, Lewis E. Kay. 2006
498 citations recorded by the source corpus.
Subfields: Materials Chemistry, Molecular Biology
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In Molecular Biology
Citations in the corpus
- Surface Plasmon Resonance: A Versatile Technique for Biosensor Applications (2015, background): “Numerous strategies for protein labeling have been developed that allow the characterization of proteins regarding their structure, folding or interaction with other proteins [1,2].”
- The structure of mouse cytomegalovirus m04 protein determined from sparse NMR data reveals a new fold of the m02-m06 family of viral immune modulators (2014, unknown): “Methyl protons are reintroduced using site-specific labeling of Ile, Leu, and Val (ILV) residues (Tugarinov et al., 2006), a scheme that greatly simplifies the NMR spectra while still providing a sparse set of long-range methyl-methyl nuclear 73, September 2, 2014 ª2014 Elsevier Ltd All rights…”
- Protein structure determination by combining sparse NMR data with evolutionary couplings (2015, unknown): “Sparse NMR data is collected using uniformly 13 C, 15 N-enriched and/or 2 H, 13 C, 15 N-enriched protein samples prepared with 1 H-13 C labeling of sidechain Leu, Val, and Ile( δ ) methyl groups 3,5,21 .”