| Literature DB >> 21136327 |
D Yang1, J R Tolman, N K Goto, L E Kay.
Abstract
A triple resonance pulse scheme is presented for recording 13Cα-1Hα one-bond dipolar couplings in 15N, 13C labeled proteins. HNCO correlation maps are generated where the carbonyl chemical shift is modulated by the 13Cα-1Hα coupling, with the two doublet components separated into individual data sets. The experiment makes use of recently described methodology whereby the protein of interest is dissolved in a dilute solution of bicelles which orient above a critical temperature, thus permitting measurement of significant couplings (Tjandra and Bax, 1997a). An application to the protein ubiquitin is described.Entities:
Year: 1998 PMID: 21136327 DOI: 10.1023/A:1008223017233
Source DB: PubMed Journal: J Biomol NMR ISSN: 0925-2738 Impact factor: 2.835