Go to content
UR Home

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


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 ...


Owner only: item control page
  1. Homepage UR

University Library

Publication Server


Publishing: oa@ur.de
0941 943 -4239 or -69394

Dissertations: dissertationen@ur.de
0941 943 -3904

Research data: datahub@ur.de
0941 943 -5707

Contact persons