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Stereospecific assignment of the NH2 resonances from the primary amides of asparagine and glutamine side chains in isotopically labeled proteins

TitleStereospecific assignment of the NH2 resonances from the primary amides of asparagine and glutamine side chains in isotopically labeled proteins
Publication TypeJournal Article
Year of Publication1997
AuthorsMcIntosh, LP, Brun, E, Kay, LE
JournalJournal of Biomolecular Nmr
Volume9
Pagination306-312
Date PublishedApr
Type of ArticleArticle
ISBN Number0925-2738
KeywordsANGLE, BACKBONE AMIDE, C-13 MAGNETIZATION, dihedral, EXCITATION, H-1, HMQC spectroscopy, LARGER PROTEINS, N-15, NMR, primary amide, SATURATION, SPECTRA, SPECTROSCOPY, STEREOSPECIFIC ASSIGNMENT
Abstract

An HMQC-based pulse scheme is presented for the stereospecific assignment of asparagine and glutamine side-chain amide protons. The approach makes use of the recently developed quantitative-J correlation spectroscopy [Bar, A. et al. (1994) Methods Enzymol., 239, 79-105] to distinguish the E and Z primary amide protons and, as such, eliminates the need for assignments derived from more time-consuming and potentially ambiguous NOE methods. An application of this method to a uniformly N-15,C-13-labeled cellulose-binding domain is presented. When used in combination with a NOESY-HSQC experiment, the predominant chi(2) dihedral angles of two asparagine side chains in this protein can also be defined.
URL<Go to ISI>://A1997XF93700008