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Temperature-Induced Transitions in Disordered Proteins Probed by NMR Spectroscopy

  • Magnus Kjaergaard
  • Flemming M. Poulsen
  • Birthe B. KragelundEmail author
Protocol
Part of the Methods in Molecular Biology book series (MIMB, volume 896)

Abstract

Intrinsically 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. NMR spectroscopy allows analysis of temperature-induced structural changes at residue resolution using secondary chemical shift analysis, paramagnetic relaxation enhancement, and residual dipolar couplings. This chapter discusses practical aspects of NMR studies of temperature-induced structural changes in disordered proteins.

Key words

Residual structure Polyproline II Chemical shift Random coil Transient helicity 

Notes

Acknowledgments

Gitte Wolfsberg Haxholm and Simon Erlendsson are thanked for critical comments on this manuscript.

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Copyright information

© Springer Science+Business Media New York 2012

Authors and Affiliations

  • Magnus Kjaergaard
    • 1
  • Flemming M. Poulsen
    • 1
  • Birthe B. Kragelund
    • 1
    Email author
  1. 1.Structural Biology and NMR Laboratory, Department of BiologyUniversity of CopenhagenCopenhagenDenmark

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