Double and Triple Resonance NMR Methods for Protein Assignment

  • Brian Whitehead
  • C. Jeremy Craven
  • Jonathan P. Waltho
Part of the Methods in Molecular Biology™ book series (MIMB, volume 60)

Abstract

Assignment of the spin systems in protein NMR spectra is an essential step in solution structure determination. The development of two-dimensional (2D) NMR experiments during the 1970s and 1980s allowed complex overlapped spectra to be unambiguously assigned for the first time, and since the mid-1980s over 100 protein solution structures have been determined by NMR. The techniques used for 1H assignment in unlabeled proteins are covered in several texts, including a previous volume in this series (1, 2, 3, 4), and will not be discussed further here. 1H homonuclear assignment strategies are usually insufficient for proteins with mol wt >10 kDa, however, and the limitations of the experiments will be outlined in the following discussion.

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Copyright information

© Humana Press Inc. 1997

Authors and Affiliations

  • Brian Whitehead
    • 1
  • C. Jeremy Craven
    • 1
  • Jonathan P. Waltho
    • 1
  1. 1.Department of Molecular Biology and BiotechnologyUniversity of SheffieldUK

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