Solving Solution Structural Problems by Combining 2-D NMR Data with Known Substructures from a Protein Database
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).
Unable to display preview. Download preview PDF.
- Phillips, D C, (1970) in British Biochemistry, Past and Present, (ed T W Goodwin) Academic Press, London, pp 11–28Google Scholar