Biochemical and Biophysical Research Communications
Proton NMR studies of the GDP.Mg2+ complex of the Ha-ras oncogene product p21
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Structural basis of the atypical activation mechanism of KRAS<sup>V14I</sup>
2019, Journal of Biological ChemistryCitation Excerpt :In the V14I mutant both interactions are lost. Also, the guanine base is typically sandwiched between Phe28 and Lys117 side chains (31), but this interaction is also lost in KRASV14I (Fig. S1). Finally, we noted electron density consistent with oxidation of the thiol at Cys118.
Probing the GTPase cycle with real-time NMR: GAP and GEF activities in cell extracts
2012, MethodsCitation Excerpt :NMR has proven to be a powerful tool for the study of enzymatic catalysis over the decades, with pioneering work by Mildred Cohn and Albert Mildevan on bacterial enzymes including pyruvate carboxylase and kinase, and alkaline phosphatase [64–66]. NMR studies on small GTPases started in the mid-1980s [67–69], but were focused on static structures and backbone dynamics of these proteins, alone or in complex with GAPs, GEFs or effectors. Real-time NMR describes a process of collecting sequential NMR spectra as a reaction or process occurs in a sample.
Handbook of growth factors: Volume I: General basic aspects
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2016, Biological ChemistryNucleotide binding and GTP hydrolysis by the 21‐kDa product of the c‐H‐ras gene as monitored by proton‐NMR spectroscopy
1993, European Journal of Biochemistry