Laura Kay

Physics

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Rennella E, Huang R, Velyvis A, et al. (2015) (13)CHD2-CEST NMR spectroscopy provides an avenue for studies of conformational exchange in high molecular weight proteins. Journal of Biomolecular Nmr. 63: 187-99
Bouvignies G, Vallurupalli P, Kay LE. (2014) Visualizing side chains of invisible protein conformers by solution NMR. Journal of Molecular Biology. 426: 763-74
LundstrÃ¶m P, Hansen DF, Vallurupalli P, et al. (2009) Accurate measurement of alpha proton chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy. Journal of the American Chemical Society. 131: 1915-26
Korzhnev DM, Kay LE. (2008) Probing invisible, low-populated States of protein molecules by relaxation dispersion NMR spectroscopy: an application to protein folding. Accounts of Chemical Research. 41: 442-51
Choy WY, Shortle D, Kay LE. (2003) Side chain dynamics in unfolded protein states: an NMR based 2H spin relaxation study of delta131delta. Journal of the American Chemical Society. 125: 1748-58
Zhang O, Forman-Kay JD, Shortle D, et al. (1997) Triple-resonance NOESY-based experiments with improved spectral resolution: Applications to structural characterization of unfolded, partially folded and folded proteins Journal of Biomolecular Nmr. 9: 181-200