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Showing 1 to 4 of 4 for “"SPROX"”.
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Development and Application of a quantitative Mass spectrometry based Platform for Thermodynamic Analysis of Protein interaction Networks
… Stability of Protein from Rates of Oxidation (SPROX) techniques, which have been previously established for the thermodynamic analysis of protein folding reactions and protein-ligand binding interactions. The work in this thesis is comprised of four parts. Part I involves the development of a …
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Development and Application of Covalent-Labeling Strategies for the Large-Scale Thermodynamic Analysis of Protein Folding and Ligand Binding
… Stability of Proteins from Rates of Oxidation (SPROX) is a recently developed mass spectrometry-based approach for proteome-wide thermodynamic stability analysis. Since the proteomic coverage of SPROX is fundamentally limited by the detection of methionine-containing peptides, the use of …
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Application and Evaluation of a Chemical Modification- and Mass Spectrometry-Based Thermodynamic Assay for the Study of Protein-Ligand Interactions in Complex Mixtures
… facilitate studies of drug action. Recently, the SPROX (stability of proteins from rates of oxidation) technique was developed as a chemical modification- and mass spectrometry-based strategy for detecting protein-ligand interactions by monitoring the change in thermodynamic stability of proteins …
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Development and Application of Large-Scale Protein Folding Stability Analysis in Drug Target Identification and Disease Biomarker Discovery
… the suglutinol A study, a combination of SPROX, TPP, CPP and STEPP-PP strategies was used to identified two consistent protein hits, deoxycytidine kinase (DCK) and exportin-2 (XPO2), from more than 2000 assayed proteins in a 2B4T cell lysate. The binding of DCK with subglutinol A was …