Analyzing temperature-induced transitions in disordered proteins by NMR spectroscopy and secondary chemical shift analyses.
Magnus Kjaergaard, Flemming M Poulsen, Birthe B Kragelund
Structural Biology and NMR Laboratory, Department of Biology, University of Copenhagen, Copenhagen, Denmark.
Methods in molecular biology (Clifton, N.J.) 2012Intrinsically disordered proteins are abundant in nature and perform many important physiological functions. Multidimensional NMR spectroscopy has been crucial for the understanding of the conformational properties of disordered proteins and is increasingly used to probe their conformational ensembles. Compared to folded proteins, disordered proteins are more malleable and more easily perturbed by environmental factors. Accordingly, the experimental conditions and especially the temperature modify the structural and functional properties of disordered proteins. This chapter discusses practical aspects of NMR studies of temperature-induced structural changes in disordered proteins using chemical shifts.
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Magnus Kjaergaard, Flemming M Poulsen, Birthe B Kragelund. Analyzing temperature-induced transitions in disordered proteins by NMR spectroscopy and secondary chemical shift analyses. Methods in molecular biology (Clifton, N.J.). 2012;896:249-56
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PMID: 22821529
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