Stumber, Michael and Geyer, Matthias and Graf, Robert and Kalbitzer, Hans Robert and Scheffzek, Klaus and Haeberlen, Ulrich (2002) Observation of slow dynamic exchange processes in Ras protein crystals by ³¹P solid state NMR spectroscopy. Journal of molecular biology 323 (5), pp. 899-907.
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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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|Institutions:||Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer|
|Dewey Decimal Classification:||500 Science > 570 Life sciences|
|Created at the University of Regensburg:||Unknown|
|Deposited On:||15 Sep 2010 09:17|
|Last Modified:||15 Sep 2010 09:17|