| Literature DB >> 20680662 |
L P McIntosh1, E Brun, L E Kay.
Abstract
An HMQC-based pulse scheme is presented for the stereospecific assignment of asparagineand glutamine side-chain amide protons. The approach makes use of the recently developedquantitative-J correlation spectroscopy [Bax, A. et al. (1994) Methods Enzymol., 239,79-105] to distinguish the E and Z primary amide protons and, as such, eliminates theneed for assignments derived from more time-consuming and potentially ambiguous NOEmethods. An application of this method to a uniformly 15N,13C-labeled cellulose-bindingdomain is presented. When used in combination with a NOESY-HSQC experiment, thepredominant chi2 dihedral angles of two asparagine side chains in this protein can also bedefined.Entities:
Year: 1997 PMID: 20680662 DOI: 10.1023/A:1018635110491
Source DB: PubMed Journal: J Biomol NMR ISSN: 0925-2738 Impact factor: 2.835