TY - JOUR
T1 - Ultra-high resolution in MAS solid-state NMR of perdeuterated proteins
T2 - Implications for structure and dynamics
AU - Reif, Bernd
N1 - Funding Information:
I am very much indepted to current and former group members, in particular Vipin Agarwal, Sam Asami, Veniamin Chevelkov, Muralidhar Dasari, Uwe Fink, Rasmus Linser and Juan Miguel Lopez del Amo for their efforts that they put into the studies of deuterated peptides and proteins in the solid-state which had been carried out over the past years. I would like to thank Alexey Krushelnitzky, Dieter Oesterheld, Hartmut Oschkinat, Detlev Reichert and Nikolai Skrynnikov for their intense collaborations and many stimulating discussions. This research was supported by the Leibniz-Gemeinschaft, the Helmholtz-Gemeinschaft, the DFG (Re1435, SFB740) and the Center for Integrated Protein Science Munich (CIPS-M).
PY - 2012/3
Y1 - 2012/3
N2 - High resolution proton spectra are obtained in MAS solid-state NMR in case samples are prepared using perdeuterated protein and D 2O in the recrystallization buffer. Deuteration reduces drastically 1H, 1H dipolar interactions and allows to obtain amide proton line widths on the order of 20 Hz. Similarly, high-resolution proton spectra of aliphatic groups can be obtained if specifically labeled precursors for biosynthesis of methyl containing side chains are used, or if limited amounts of H 2O in the bacterial growth medium is employed. This review summarizes recent spectroscopic developments to access structure and dynamics of biomacromolecules in the solid-state, and shows a number of applications to amyloid fibrils and membrane proteins.
AB - High resolution proton spectra are obtained in MAS solid-state NMR in case samples are prepared using perdeuterated protein and D 2O in the recrystallization buffer. Deuteration reduces drastically 1H, 1H dipolar interactions and allows to obtain amide proton line widths on the order of 20 Hz. Similarly, high-resolution proton spectra of aliphatic groups can be obtained if specifically labeled precursors for biosynthesis of methyl containing side chains are used, or if limited amounts of H 2O in the bacterial growth medium is employed. This review summarizes recent spectroscopic developments to access structure and dynamics of biomacromolecules in the solid-state, and shows a number of applications to amyloid fibrils and membrane proteins.
KW - H labeling
KW - Magic Angle Spinning (MAS) solid-state NMR
KW - Microcrystalline proteins
KW - N relaxation
KW - Order parameters
KW - Perdeuteration
KW - Protein dynamics
UR - http://www.scopus.com/inward/record.url?scp=84858333634&partnerID=8YFLogxK
U2 - 10.1016/j.jmr.2011.12.017
DO - 10.1016/j.jmr.2011.12.017
M3 - Article
C2 - 22280934
AN - SCOPUS:84858333634
SN - 1090-7807
VL - 216
SP - 1
EP - 12
JO - Journal of Magnetic Resonance
JF - Journal of Magnetic Resonance
ER -