C
Christian Griesinger
Researcher at Max Planck Society
Publications - 449
Citations - 25595
Christian Griesinger is an academic researcher from Max Planck Society. The author has contributed to research in topics: Nuclear magnetic resonance spectroscopy & Residual dipolar coupling. The author has an hindex of 76, co-authored 408 publications receiving 23162 citations. Previous affiliations of Christian Griesinger include University of Göttingen & ETH Zurich.
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Journal ArticleDOI
A New Experiment for the Measurement of nJ(C,P) Coupling Constants Including 3J(C4'i,Pi) and 3J(C4'i,Pi+1) in Oligonucleotides.
Christian Richter,Bernd Reif,Karlheinz Wörner,Stefanie Quant,John P. Marino,Joachim W. Engels,Christian Griesinger,Harald Schwalbe +7 more
TL;DR: A new experiment for the measurement of nJ(C,P) coupling constants along the phosphodiester backbone in RNA and DNA based on a quantitative-J HCP experiment is presented, and the backbone angles β and ∈ can be determined.
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Thermal coefficients of the methyl groups within ubiquitin
T. Michael Sabo,Davood Bakhtiari,Korvin F. A. Walter,Robert L. McFeeters,Karin Giller,Stefan Becker,Christian Griesinger,Donghan Lee +7 more
TL;DR: By analyzing the distribution of methyl group thermal coefficients within ubiquitin, it is found that the N‐terminal region has relatively high thermostability, and results indicate that methyl groups contribute quite appreciably to the total heat capacity of ubiquit in through the regulation of local conformational entropy.
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Simultaneous determination of fast and slow dynamics in molecules using extreme CPMG relaxation dispersion experiments.
Jithender G. Reddy,Supriya Pratihar,David Ban,Sebastian Frischkorn,Stefan Becker,Christian Griesinger,Donghan Lee +6 more
TL;DR: Using a fast folding protein, gpW, it is shown that previously inaccessible kinetics can be accessed with the improved precision and efficiency of the measurement by using this experiment.
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Residual dipolar coupling enhanced NMR spectroscopy and chiroptics: a powerful combination for the complete elucidation of symmetrical small molecules.
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Catalytic mechanism of the metal-free hydrogenase from methanogenic archaea : reversed stereospecificity of the catalytic and noncatalytic reaction
Bernhard H. Geierstanger,Thomas Prasch,Christian Griesinger,Gudrun C. Hartmann,Gerrit Buurman,Rolf K. Thauer +5 more
TL;DR: According to NMR spectroscopic analysis of the conformation of the hydrogen acceptor in solution, in the enzyme-catalyzed reaction the hydrogenation product is formed in a constraint conformation which relaxes upon dissociation from the enzyme.