Abstract
Two-dimensional nuclear magnetic resonance (2D-NMR) spectroscopy is a powerful method for studying the three-dimensional structure of small and medium-sized proteins (MW < 10 kD) in solution (Wüthrich et al 1982). Proteins studied by this method include micelle-bound glucagon (Braun et al 1983), lac repressor headpiece (Kaptein et al 1985, Zuiderweg et al 1983), cAMP receptor protein helix F (Clore et al 1985) and bull seminal plasma inhibitor IIA (Williamson et al 1985).
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© 1987 Springer-Verlag Berlin Heidelberg
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Kraulis, P.J., Jones, T.A. (1987). Solving Solution Structural Problems by Combining 2-D NMR Data with Known Substructures from a Protein Database. In: Ehrenberg, A., Rigler, R., Gräslund, A., Nilsson, L. (eds) Structure, Dynamics and Function of Biomolecules. Springer Series in Biophysics, vol 1. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71705-5_25
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DOI: https://doi.org/10.1007/978-3-642-71705-5_25
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