Temperature-induced transitions in disordered proteins probed by NMR spectroscopy

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

  • Magnus Kjærgaard
  • Flemming Martin Poulsen, Biomolecular Sciences, Danmark
  • Birthe Brandt Kragelund, Biomolecular Sciences, Danmark
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.
OriginalsprogEngelsk
TidsskriftMethods in molecular biology (Clifton, N.J.)
Vol/bind896
Sider (fra-til)233-47
Antal sider15
ISSN1064-3745
DOI
StatusUdgivet - 2012
Eksternt udgivetJa

Se relationer på Aarhus Universitet Citationsformater

ID: 70230746