title: Solution-state nuclear magnetic resonance spectroscopy and protein folding.
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.
authors.affiliation: Department of Structural and Molecular Biology, University College London, London, UK.
authors.forename: Lisa D
authors.initials: LD
authors.lastname: Cabrita
authors.forename: Christopher A
authors.initials: CA
authors.lastname: Waudby
authors.forename: Christopher M
authors.initials: CM
authors.lastname: Dobson
authors.forename: John
authors.initials: J
authors.lastname: Christodoulou
mesh_terms: D053000:Analytic Sample Preparation Methods; D003903:Deuterium / Q000737:chemistry; D041961:Deuterium Exchange Measurement; D004058:Diffusion; D057446:Hydrodynamics; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D011522:Protons; D012996:Solutions; D012997:Solvents / Q000737:chemistry; D013113:Spin Labels; D013194:Staining and Labeling
chemical_list: D011506:Proteins; D011522:Protons; D012996:Solutions; D012997:Solvents; D013113:Spin Labels; D003903:Deuterium