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Pressure Dependence of 15N Chemical Shifts in Model Peptides Ac-Gly-Gly-X-Ala-NH2

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Koehler, Joerg ; Beck Erlach, Markus ; Crusca, Edson ; Kremer, Werner ; Munte, Claudia Elisabeth ; Kalbitzer, Hans Robert
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Date of publication of this fulltext: 12 Feb 2014 10:46


High pressure NMR spectroscopy has developed into an important tool for studying conformational equilibria of proteins in solution. We have studied the amide proton and nitrogen chemical shifts of the 20 canonical amino acids X in the random-coil model peptide Ac-Gly-Gly-X-Ala-NH2, in a pressure range from 0.1 to 200 MPa, at a proton resonance frequency of 800 MHz. The obtained data allowed the ...


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