ArticleAnalytical biochemistry2021
Ras-guanine nucleotide complexes: A UV spectral deconvolution method to analyze protein concentration, nucleotide stoichiometry, and purity.
Article in Analytical biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed, 3 citations in OpenAlex.
- Binding of active Ras and its mutants to the Ras binding domain of PI-3-kinase: A quantitative approach to KAnalytical biochemistry · 2023Article
- HPLC method to resolve, identify and quantify guanine nucleotides bound to recombinant ras GTPase.Analytical biochemistry · 2021Article
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5 authors at 1 institution in 1 country.
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Abstract
The many members of the Ras superfamily are small GTPases that serve as molecular switches. These proteins bind the guanine nucleotides GTP and GDP with picomolar affinities, thereby stabilizing on- and off-signaling states, respectively. Quantitative in vitro Ras studies require accurate determination of total protein, its fractional occupancy with guanine nucleotide, and spectroscopic purity. Yet the high nucleotide affinity of Ras and the overlapping UV spectra of the protein and bound nucleotide make such determinations challenging. Here we describe a generalizable UV spectral deconvolution method to analyze the total protein concentration, total nucleotide stoichiometry, and purity of Ras complexes.
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