Phenacyl Bromide

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Michael C Fitzgerald - One of the best experts on this subject based on the ideXlab platform.

  • targeted mass spectrometry based approach for protein ligand binding analyses in complex biological mixtures using a Phenacyl Bromide modification strategy
    Analytical Chemistry, 2016
    Co-Authors: Dongyu Wang, David M Gooden, Carol H Ball, Michael C Fitzgerald
    Abstract:

    The characterization of protein folding stability changes on the proteomic scale is useful for protein-target discovery and for the characterization of biological states. The Stability of Proteins from Rates of Oxidation (SPROX) technique is one of several mass spectrometry-based techniques recently established for the making proteome-wide measurements of protein folding and stability. A critical part of proteome-wide applications of SPROX is the identification and quantitation of methionine-containing peptides. Demonstrated here is a targeted mass spectrometry-based proteomics strategy for the detection and quantitation of methionine-containing peptides in SPROX experiments. The strategy involves the use of Phenacyl Bromide (PAB) for the targeted detection and quantitation of methionine-containing peptides in SPROX using selective reaction monitoring (SRM) on a triple quadrupole mass spectrometer (QQQ-MS). As proof-of-principle, the known binding interaction of Cyclosporine A with cyclophilin A protein i...

  • Targeted Mass Spectrometry-Based Approach for Protein–Ligand Binding Analyses in Complex Biological Mixtures Using a Phenacyl Bromide Modification Strategy
    Analytical Chemistry, 2016
    Co-Authors: Dongyu Wang, David M Gooden, Carol H Ball, Michael C Fitzgerald
    Abstract:

    The characterization of protein folding stability changes on the proteomic scale is useful for protein-target discovery and for the characterization of biological states. The Stability of Proteins from Rates of Oxidation (SPROX) technique is one of several mass spectrometry-based techniques recently established for the making proteome-wide measurements of protein folding and stability. A critical part of proteome-wide applications of SPROX is the identification and quantitation of methionine-containing peptides. Demonstrated here is a targeted mass spectrometry-based proteomics strategy for the detection and quantitation of methionine-containing peptides in SPROX experiments. The strategy involves the use of Phenacyl Bromide (PAB) for the targeted detection and quantitation of methionine-containing peptides in SPROX using selective reaction monitoring (SRM) on a triple quadrupole mass spectrometer (QQQ-MS). As proof-of-principle, the known binding interaction of Cyclosporine A with cyclophilin A protein i...

Padma L Nayak - One of the best experts on this subject based on the ideXlab platform.

Danyi Wu - One of the best experts on this subject based on the ideXlab platform.

Dongyu Wang - One of the best experts on this subject based on the ideXlab platform.

  • targeted mass spectrometry based approach for protein ligand binding analyses in complex biological mixtures using a Phenacyl Bromide modification strategy
    Analytical Chemistry, 2016
    Co-Authors: Dongyu Wang, David M Gooden, Carol H Ball, Michael C Fitzgerald
    Abstract:

    The characterization of protein folding stability changes on the proteomic scale is useful for protein-target discovery and for the characterization of biological states. The Stability of Proteins from Rates of Oxidation (SPROX) technique is one of several mass spectrometry-based techniques recently established for the making proteome-wide measurements of protein folding and stability. A critical part of proteome-wide applications of SPROX is the identification and quantitation of methionine-containing peptides. Demonstrated here is a targeted mass spectrometry-based proteomics strategy for the detection and quantitation of methionine-containing peptides in SPROX experiments. The strategy involves the use of Phenacyl Bromide (PAB) for the targeted detection and quantitation of methionine-containing peptides in SPROX using selective reaction monitoring (SRM) on a triple quadrupole mass spectrometer (QQQ-MS). As proof-of-principle, the known binding interaction of Cyclosporine A with cyclophilin A protein i...

  • Targeted Mass Spectrometry-Based Approach for Protein–Ligand Binding Analyses in Complex Biological Mixtures Using a Phenacyl Bromide Modification Strategy
    Analytical Chemistry, 2016
    Co-Authors: Dongyu Wang, David M Gooden, Carol H Ball, Michael C Fitzgerald
    Abstract:

    The characterization of protein folding stability changes on the proteomic scale is useful for protein-target discovery and for the characterization of biological states. The Stability of Proteins from Rates of Oxidation (SPROX) technique is one of several mass spectrometry-based techniques recently established for the making proteome-wide measurements of protein folding and stability. A critical part of proteome-wide applications of SPROX is the identification and quantitation of methionine-containing peptides. Demonstrated here is a targeted mass spectrometry-based proteomics strategy for the detection and quantitation of methionine-containing peptides in SPROX experiments. The strategy involves the use of Phenacyl Bromide (PAB) for the targeted detection and quantitation of methionine-containing peptides in SPROX using selective reaction monitoring (SRM) on a triple quadrupole mass spectrometer (QQQ-MS). As proof-of-principle, the known binding interaction of Cyclosporine A with cyclophilin A protein i...

Pramod K Nayak - One of the best experts on this subject based on the ideXlab platform.