Protein Folding, Misfolding, and Disease pp 97-120

Part of the Methods in Molecular Biology book series (MIMB, volume 752)

Solution-State Nuclear Magnetic Resonance Spectroscopy and Protein Folding

  • Lisa D. Cabrita
  • Christopher A. Waudby
  • Christopher M. Dobson
  • John Christodoulou
Protocol

Abstract

A protein undergoes a variety of structural changes during its folding and misfolding and a knowledge of its behaviour is key to understanding the molecular details of these events. Solution-state NMR spectroscopy is unique in that it can provide both structural and dynamical information at both high-resolution and at a residue-specific level, and is particularly useful in the study of dynamic systems. In this chapter, we describe NMR strategies and how they are applied in the study of protein folding and misfolding.

Key words

NMR spectroscopy Protein folding Isotopic labelling H/D exchange HSQC Diffusion 

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Copyright information

© Springer Science+Business Media, LLC 2011

Authors and Affiliations

  • Lisa D. Cabrita
  • Christopher A. Waudby
  • Christopher M. Dobson
  • John Christodoulou
    • 1
    • 2
  1. 1.Department of Structural and Molecular BiologyUniversity College LondonLondonUK
  2. 2.School of CrystallographyBirkbeck CollegeLondonUK

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