ArticleProteins2011
A miniaturized technique for assessing protein thermodynamics and function using fast determination of quantitative cysteine reactivity.
Article in Proteins, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 32 citations in OpenAlex.
- Cys-labeling kinetics of membrane protein GlpG: a role for specific SDS binding and micelle changes?Biophysical journal · 2021Article
- High-Throughput Kinetic Analysis for Target-Directed Covalent Ligand Discovery.Angewandte Chemie (International ed. in English) · 2018Article
- Tyrosine phosphorylation switching of a G protein.The Journal of biological chemistry · 2018Article
- Coordinated regulation of intracellular pH by two glucose-sensing pathways in yeast.The Journal of biological chemistry · 2018Article
- Regulation of Ras Paralog Thermostability by Networks of Buried Ionizable Groups.Biochemistry · 2016Article
- The experimental power of FR900359 to study Gq-regulated biological processes.Nature communications · 2015Article
- Redox regulation of Rac1 by thiol oxidation.Free radical biology & medicine · 2015Article
- Phosphorylation at Y1065 in vinculin mediates actin bundling, cell spreading, and mechanical responses to force.Biochemistry · 2014Article
- Guanine nucleotide-binding protein (Gα) endocytosis by a cascade of ubiquitin binding domain proteins is required for sustained morphogenesis and proper mating in yeast.The Journal of biological chemistry · 2014Article
- Biophysical and proteomic characterization strategies for cysteine modifications in Ras GTPases.Methods in molecular biology (Clifton, N.J.) · 2014Article
- Differences in the regulation of K-Ras and H-Ras isoforms by monoubiquitination.The Journal of biological chemistry · 2013Article
- Protons as second messenger regulators of G protein signaling.Molecular cell · 2013Article
- Expanding the number of 'druggable' targets: non-enzymes and protein-protein interactions.Chemical biology & drug design · 2013Review
- Site-specific monoubiquitination activates Ras by impeding GTPase-activating protein function.Nature structural & molecular biology · 2013Article
- Differences in intradomain and interdomain motion confer distinct activation properties to structurally similar Gα proteins.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Quantitation of protein-protein interactions by thermal stability shift analysis.Protein science : a publication of the Protein Society · 2011Article
- Protein stability by number: high-throughput and statistical approaches to one of protein science's most difficult problems.Current opinion in chemical biology · 2011Review
- Functional reconstitution of an atypical G protein heterotrimer and regulator of G protein signaling protein (RGS1) from Arabidopsis thaliana.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Protein thermodynamic stability is a fundamental physical characteristic that determines biological function. Furthermore, alteration of thermodynamic stability by macromolecular interactions or biochemical modifications is a powerful tool for assessing the relationship between protein structure, stability, and biological function. High-throughput approaches for quantifying protein stability are beginning to emerge that enable thermodynamic measurements on small amounts of material, in short periods of time, and using readily accessible instrumentation. Here we present such a method, fast quantitative cysteine reactivity, which exploits the linkage between protein stability, sidechain protection by protein structure, and structural dynamics to characterize the thermodynamic and kinetic properties of proteins. In this approach, the reaction of a protected cysteine and thiol-reactive fluorogenic indicator is monitored over a gradient of temperatures after a short incubation time. These labeling data can be used to determine the midpoint of thermal unfolding, measure the temperature dependence of protein stability, quantify ligand-binding affinity, and, under certain conditions, estimate folding rate constants. Here, we demonstrate the fQCR method by characterizing these thermodynamic and kinetic properties for variants of Staphylococcal nuclease and E. coli ribose-binding protein engineered to contain single, protected cysteines. These straightforward, information-rich experiments are likely to find applications in protein engineering and functional genomics.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.