Solving Solution Structural Problems by Combining 2-D NMR Data with Known Substructures from a Protein Database

  • Per J. Kraulis
  • T. Alwyn Jones
Part of the Springer Series in Biophysics book series (BIOPHYSICS, volume 1)


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).


Retinol Binding Protein Distance Constraint Nuclear Overhauser Effect Natural Science Research Council Swedish Natural Science Research Council 
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Copyright information

© Springer-Verlag Berlin Heidelberg 1987

Authors and Affiliations

  • Per J. Kraulis
    • 1
  • T. Alwyn Jones
    • 1
  1. 1.Department of Molecular Biology, Biomedical Centre, BMCUniversity of UppsalaUppsalaSweden

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