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

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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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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Item Type:Article
Date:2002
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
12417202PubMed ID
Classification:
NotationType
Binding SitesMESH
CrystallizationMESH
Crystallography, X-RayMESH
Guanylyl Imidodiphosphate/chemistryMESH
Models, MolecularMESH
Nuclear Magnetic Resonance, Biomolecular/methodsMESH
PhosphorusMESH
Protein ConformationMESH
ThermodynamicsMESH
ras Proteins/chemistryMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:15 Sep 2010 09:17
Last Modified:15 Sep 2010 09:17
Item ID:16588
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