Analyzing temperature-induced transitions in disordered proteins by NMR spectroscopy and secondary chemical shift analyses

Magnus Kjærgaard, Flemming Martin Poulsen, Birthe Brandt Kragelund

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

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. This chapter discusses practical aspects of NMR studies of temperature-induced structural changes in disordered proteins using chemical shifts.
Original languageEnglish
JournalMethods in molecular biology (Clifton, N.J.)
Volume896
Pages (from-to)249-56
Number of pages8
ISSN1064-3745
DOIs
Publication statusPublished - 2012
Externally publishedYes

Keywords

  • Analytic Sample Preparation Methods
  • Calibration
  • Nuclear Magnetic Resonance, Biomolecular
  • Proteins
  • Temperature

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