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1.
Softley, C. ; Bostock, M.J. ; Popowicz, G.M. & Sattler, M.: Paramagnetic NMR in drug discovery. J. Biomol. NMR 74, 287–309 (2020)
2.
Tripsianes, K.* ; Schütz, U. ; Emmanouilidis, L. ; Gemmecker, G. & Sattler, M.: Selective isotope labeling for NMR structure determination of proteins in complex with unlabeled ligands. J. Biomol. NMR 73, 183-189 (2019)
3.
Xue, K. ; Mamone, S.* ; Koch, B. ; Sarkar, R. & Reif, B.: Determination of methyl order parameters using solid state NMR under off magic angle spinning. J. Biomol. NMR 73, 471-475 (2019)
4.
Xue, K. et al.: MAS dependent sensitivity of different isotopomers in selectively methyl protonated protein samples in solid state NMR. J. Biomol. NMR 73, 625-631 (2019)
5.
Chevelkov, V.* et al.: Perspectives for sensitivity enhancement in proton-detected solid-state NMR of highly deuterated proteins by preserving water magnetization. J. Biomol. NMR 61, 151-160 (2015)
6.
Freiburger, L. et al.: Efficient segmental isotope labeling of multi-domain proteins using Sortase A. J. Biomol. NMR 63, 1-8 (2015)
7.
Lange, O.F.: Automatic NOESY assignment in CS-RASREC-Rosetta. J. Biomol. NMR 59, 147-159 (2014)
8.
Linser, R.* ; Sarkar, R. ; Krushelnitzky, A.* ; Mainz, A. & Reif, B.: Dynamics in the solid-state: Perspectives for the investigation of amyloid aggregates, membrane proteins and soluble protein complexes. J. Biomol. NMR 59, 1-14 (2014)
9.
Lopez del Amo, J.M. et al.: Site-specific analysis of heteronuclear Overhauser effects in microcrystalline proteins. J. Biomol. NMR 59, 241-249 (2014)
10.
Zhang, Z.* ; Porter, J.* ; Tripsianes, K.* & Lange, O.F.: Robust and highly accurate automatic NOESY assignment and structure determination with Rosetta. J. Biomol. NMR 59, 135-145 (2014)
11.
Hennig, J. ; Wang, I. ; Sonntag, M. ; Gabel, F.* & Sattler, M.: Combining NMR and small angle X-ray and neutron scattering in the structural analysis of a ternary protein-RNA complex. J. Biomol. NMR 56, 17-30 (2013)
12.
Lopez del Amo, J.M. ; Schneider, D.* ; Loquet, A.* ; Lange, A.* & Reif, B.: Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-β peptide: Perspectives for DNP. J. Biomol. NMR 56, 359-363 (2013)
13.
van der Schot, G.* et al.: Improving 3D structure prediction from chemical shift data. J. Biomol. NMR 57, 27-35 (2013)
14.
Vernon, R.* ; Shen, Y.* ; Baker, D.* & Lange, O.F.: Improved chemical shift based fragment selection for CS-Rosetta using Rosetta3 fragment picker. J. Biomol. NMR 57, 117-127 (2013)
15.
Asami, S.* & Reif, B.: Assignment strategies for aliphatic protons in the solid-state in randomly protonated proteins. J. Biomol. NMR 52, 31-39 (2012)
16.
Asami, S. ; Szekely, K.* ; Schanda, P.* ; Meier, B.H.* & Reif, B.: Optimal degree of protonation for 1H detection of aliphatic sites in randomly deuterated proteins as a function of the MAS frequency. J. Biomol. NMR 54, 155-168 (2012)
17.
Lopez del Amo, J.M.* ; Fink, U.* & Reif, B.: Quantification of protein backbone hydrogen-deuterium exchange rates by solid state NMR spectroscopy. J. Biomol. NMR 48, 203-212 (2010)
18.
Gabel, F.* et al.: A structure refinement protocol combining NMR residual dipolar couplings and small angle scattering restraints. J. Biomol. NMR 41, 199-208 (2008)
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