Del i serien Methods in Molecular Biology

Histidine Phosphorylation

Methods and Protocols

Häftad, Engelska, 2020

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This volume details the current understanding of roles and regulation on histidine phosphorylation, describing methods for the characterization of protein phosphorylation on histidine.

Produktinformation

Utgivningsdatum2020-11-10
Mått178 x 254 x 15 mm
Vikt511 g
FormatHäftad
SpråkEngelska
SerieMethods in Molecular Biology
Antal sidor256
FörlagHumana Press Inc.
ISBN9781493998869

Tillhör följande kategorier

Biokemi inom Naturvetenskap och teknik

Protein Dynamics in Phosphoryl-transfer Signaling Mediated by Two-component Systems.- A High-throughput Strategy for Recombinant Protein Expression and Solubility Screening in Escherichia coli – A Case of Sensor Histidine Kinase.- SDS-PAGE and Dot Blot Autoradiography: Tools for Quantifying Histidine Kinase Autophosphorylation.- A Quantitative Method for the Measurement of Protein Histidine Phosphorylation.- Analysis of 1- and 3-phosphohistidine (pHis) Protein Modification using Model Enzymes Expressed in Bacteria.- Determination of Phosphohistidine Stoichiometry in Histidine Kinases by Intact Mass Spectrometry.- Protein Phosphohistidine Phosphatases of the HP Superfamily.- In Vitro Assays for Measuring Protein Histidine Phosphatase Activity.- Structural and Functional Characterization of Autophosphorylation in Bacterial Histidine Kinases.- Manipulation of Bacterial Signalling using Engineered Histidine Kinases.- Development of a Light-Dependent Protein Histidine Kinase.- Empirical Evidence of Cellular Histidine Phosphorylation by Immunoblotting using pHis mAbs.- Immunohistochemistry (IHC): Chromogenic Detection of 3-Phosphohistidine Proteins in Formaldehyde-Fixed, Frozen Mouse Liver Tissue Sections.- Subcellular Localisation of Histidine Phosphorylated Proteins through Indirect Immunofluorescence.- High throughput Characterisation of Histidine Phosphorylation sites using UPAX and Tandem Mass Spectrometry.- Proteome Bioinformatics Methods for Studying Histidine Phosphorylation.