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Article10.1007/978-1-60327-223-0_7

Solution-State Nuclear Magnetic Resonance Spectroscopy and Protein Folding

Lisa D. Cabrita,Christopher A. Waudby,Christopher M. Dobson,John Christodoulou-2011-01-01-Methods in molecular biology
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TL;DRAbstract

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.

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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.

Keywords

Protein foldingNuclear magnetic resonance spectroscopyFolding (DSP implementation)SpectroscopyChemical physicsChemistryNative stateHigh resolution

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