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Biophysical Chemistry|August 24, 2019
The pressure and temperature perturbation approach reveals a whole variety of conformational substates of amyloidogenic hIAPP monitored by 2D NMR spectroscopyMarkus Beck Erlach, Hans Robert Kalbitzer, Roland Winter, et al.Journal of Molecular Biology|June 17, 2023
Insights into the Structure of Invisible Conformations of Large Methyl Group Labeled Molecular Machines from High Pressure NMRChristina Krempl, Jan Philip Wurm, Markus Beck Erlach, et al.Lipids in Health and Disease|March 25, 2023
NMR derived changes of lipoprotein particle concentrations related to impaired fasting glucose, impaired glucose tolerance, or manifest type 2 diabetes mellitusTina Kalbitzer, Kristina Lobenhofer, Silke Martin, et al.The Journal of Physical Chemistry. B|May 7, 2014
Relationship between nonlinear pressure-induced chemical shift changes and thermodynamic parametersMarkus Beck Erlach, Joerg Koehler, Beate Moeser, et al.Journal of Biomolecular NMR|June 24, 2016
Pressure dependence of backbone chemical shifts in the model peptides Ac-Gly-Gly-Xxx-Ala-NH2Markus Beck Erlach, Joerg Koehler, Edson Crusca, et al.Journal of Magnetic Resonance (San Diego, Calif. : 1997)|April 3, 2010
Ceramic cells for high pressure NMR spectroscopy of proteinsMarkus Beck Erlach, Claudia E Munte, Werner Kremer, et al.Journal of Biomolecular NMR|June 24, 2020
Pressure dependence of side chain <sup>1</sup>H and <sup>15</sup>N-chemical shifts in the model peptides Ac-Gly-Gly-Xxx-Ala-NH<sub>2</sub>Markus Beck Erlach, Joerg Koehler, Claudia E Munte, et al.Journal of Biomolecular NMR|August 14, 2014
Pressure response of amide one-bond J-couplings in model peptides and proteinsJoerg Koehler, Markus Beck Erlach, Edson Crusca, et al.Journal of Biomolecular NMR|September 16, 2017
Pressure dependence of side chain <sup>13</sup>C chemical shifts in model peptides Ac-Gly-Gly-Xxx-Ala-NH<sub>2</sub>Markus Beck Erlach, Joerg Koehler, Edson Crusca, et al.Journal of the American Chemical Society|July 22, 2011
Pulsed pressure perturbations, an extra dimension in NMR spectroscopy of proteinsWerner Kremer, Martin Arnold, Claudia Elisabeth Munte, et al.Pageof 2