caa a22 4500 477136389 CHVBK 20180405111719.0 cr unu---uuuuu 170330e19970401xx s 000 0 eng 10.1023/A:1018635110491 doi (NATIONALLICENCE)springer-10.1023/A:1018635110491 Stereospecific assignment of the NH2 resonances from the primary amides of asparagine and glutamine side chains in isotopically labeled proteins [Elektronische Daten] [Lawrence McIntosh, Emmanuel Brun, Lewis Kay] 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 χ2 dihedral angles of two asparagine side chains in this protein can also bedefined. Kluwer Academic Publishers, 1997 Primary amide nationallicence Stereospecific assignment nationallicence HMQC spectroscopy nationallicence Dihedral angle nationallicence McIntosh Lawrence Protein Engineering Network Centers of Excellence, Department of Biochemistry and Molecular Biology and Department of Chemistry, University of British Columbia, V6T 1Z3, Vancouver, BC, Canada aut Brun Emmanuel Protein Engineering Network Centers of Excellence, Department of Biochemistry and Molecular Biology and Department of Chemistry, University of British Columbia, V6T 1Z3, Vancouver, BC, Canada aut Kay Lewis Protein Engineering Network Centers of Excellence and Departments of Medical Genetics, Biochemistry and Chemistry, University of Toronto, M5S 1A8, Toronto, ON, Canada aut Journal of Biomolecular NMR Kluwer Academic Publishers 9/3(1997-04-01), 306-312 0925-2738 9:3<306 1997 9 10858 https://doi.org/10.1023/A:1018635110491 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1018635110491 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- McIntosh Lawrence Protein Engineering Network Centers of Excellence, Department of Biochemistry and Molecular Biology and Department of Chemistry, University of British Columbia, V6T 1Z3, Vancouver, BC, Canada aut NATIONALLICENCE 700 1- Brun Emmanuel Protein Engineering Network Centers of Excellence, Department of Biochemistry and Molecular Biology and Department of Chemistry, University of British Columbia, V6T 1Z3, Vancouver, BC, Canada aut NATIONALLICENCE 700 1- Kay Lewis Protein Engineering Network Centers of Excellence and Departments of Medical Genetics, Biochemistry and Chemistry, University of Toronto, M5S 1A8, Toronto, ON, Canada aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Kluwer Academic Publishers 9/3(1997-04-01), 306-312 0925-2738 9:3<306 1997 9 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer