TY - JOUR
T1 - Temperature-induced transitions in disordered proteins probed by NMR spectroscopy
AU - Kjærgaard, Magnus
AU - Poulsen, Flemming Martin
AU - Kragelund, Birthe Brandt
PY - 2012
Y1 - 2012
N2 - 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.
AB - 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.
KW - Humans
KW - Nuclear Magnetic Resonance, Biomolecular
KW - Proteins
KW - Temperature
U2 - 10.1007/978-1-4614-3704-8_15
DO - 10.1007/978-1-4614-3704-8_15
M3 - Journal article
C2 - 22821528
SN - 1064-3745
VL - 896
SP - 233
EP - 247
JO - Methods in molecular biology (Clifton, N.J.)
JF - Methods in molecular biology (Clifton, N.J.)
ER -