期刊
JOURNAL OF BIOMOLECULAR NMR
卷 51, 期 3, 页码 329-337出版社
SPRINGER
DOI: 10.1007/s10858-011-9560-y
关键词
Lanthanides; Pseudocontact shifts; Residual dipolar couplings; Paramagnetic NMR
资金
- Max Planck Society
- Netherlands Foundation for Scientific Research (NWO-CW)
- European Union [261863, 228461]
Here we present Cys-Ph-TAHA, a new nonadentate lanthanide tag for the paramagnetic labelling of proteins. The tag can be easily synthesized and is stereochemically homogenous over a wide range of temperatures, yielding NMR spectra with a single set of peaks. Bound to ubiquitin, it induced large residual dipolar couplings and pseudocontact shifts that could be measured easily and agreed very well with the protein structure. We show that Cys-Ph-TAHA can be used to label large proteins that are biochemically challenging such as the Lac repressor in a 90 kDa ternary complex with DNA and inducer.
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