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Observation of slow dynamic exchange processes in Ras protein crystals by ³¹P solid state NMR spectroscopy

Stumber, Michael ; Geyer, Matthias ; Graf, Robert ; Kalbitzer, Hans Robert ; Scheffzek, Klaus ; Haeberlen, Ulrich



Abstract

The folding, structure and biological function of many proteins are inherently dynamic properties of the protein molecule. Often, the respective molecular processes are preserved upon protein crystallization, leading, in X-ray diffraction experiments, to a blurring of the electron density map and reducing the resolution of the derived structure. Nuclear magnetic resonance (NMR) is known to be an ...

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