@article{c6fe3953e8fc441b872d52ba7da1b068,
title = "A sensitive pulse scheme for measuring the backbone dihedral angle ψ based on cross-correlation between 13Cα-1Hα dipolar and carbonyl chemical shift anisotropy relaxation interactions",
abstract = "A pulse scheme for measuring cross-correlation between 13Cα-1Hα dipolar and carbonyl chemical shift anisotropy relaxation mechanisms is presented from which the protein backbone dihedral angle ψ is measured. The method offers significant sensitivity gains relative to our recently published scheme for measuring ψ based on this cross-correlation effect [Yang et al. (1997) J. Am. Chem. Soc., 119, 11938-11940]. The utility of the method is demonstrated with an application to a 42 kDa complex of 15N,13C-labeled maltose binding protein and β-cyclodextrin.",
keywords = "Chemical shift anisotropy, Cross-correlation, Psi",
author = "Daiwen Yang and Gardner, {Kevin H.} and Kay, {Lewis E.}",
note = "Funding Information: The authors are grateful to Professors J. Wand (SUNY, Buffalo) and Rick Dahlquist (University of Oregon) for kindly supplying the 15N,13C-labeled samples of ubiquitin and CheY used in this study, to Professor Kalle Gehring (McGill University) for providing the maltose binding protein plasmid, and to Mr. Randall Willis (Hospital for Sick Children) for preparation of the maltose binding protein sample. This research was supported by the Medical Research Council of Canada. L.E.K. is an International Howard Hughes Research Scholar. K.H.G. was supported by a post- doctoral fellowship from the Helen Hey Whitney Foundation.",
year = "1998",
doi = "10.1023/A:1008284315816",
language = "English (US)",
volume = "11",
pages = "213--220",
journal = "Journal of biomolecular NMR",
issn = "0925-2738",
publisher = "Springer Netherlands",
number = "2",
}