Temperature-induced transitions in disordered proteins probed by NMR spectroscopy

Magnus Kjærgaard, Flemming Martin Poulsen, Birthe Brandt Kragelund

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


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.
Original languageEnglish
JournalMethods in molecular biology (Clifton, N.J.)
Pages (from-to)233-47
Number of pages15
Publication statusPublished - 2012
Externally publishedYes


  • Humans
  • Nuclear Magnetic Resonance, Biomolecular
  • Proteins
  • Temperature


Dive into the research topics of 'Temperature-induced transitions in disordered proteins probed by NMR spectroscopy'. Together they form a unique fingerprint.

Cite this