Slow conformational dynamics of the guanine nucleotide-binding protein Ras complexed with the GTP analogue GTPγS
Author:
Publisher
Wiley
Subject
Cell Biology,Molecular Biology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1742-4658.2007.05681.x/fullpdf
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2. Conformational states of Ras complexed with the GTP-analogs GppNHp or GppCH2p: implications for the interaction with effector proteins;Spoerner;Biochemistry,2005
3. Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy;Kraulis;Biochemistry,1994
4. Regional polysterism in the GTP-bound form of the human c-Ha-Ras protein;Ito;Biochemistry,1997
5. Observation of slow dynamic exchange processes in Ras protein crystals by 31P solid state NMR spectroscopy;Stumber;J Mol Biol,2002
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