Titlebook: SH2 Domains; Methods and Protocol Kazuya Machida,Bernard A. Liu Book 2017 Springer Science+Business Media LLC 2017 receptor tyrosine kinase

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Structural Characterization of Monomeric/Dimeric State of p59fyn SH2 Domain Despite the fact that SH2 domains acquire their biological functions in a monomeric state, a multitude of reports have shown their tendency to dimerize. Here, we provide a technical description on how to isolate and characterize by gel filtration, circular dichroism (CD), and nuclear magnetic reson

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NMR Chemical Shift Mapping of SH2 Peptide Interactionsng and conformational insights into a protein–peptide interaction. By tracking .H and .N chemical shift changes over the course of a peptide titration into isotopically labeled protein, amide NH pairs of amino acids whose chemical environment changes upon peptide binding can be identified. When mapp

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Book 2017I outlines the history of SH2, technology development, and cell signaling; Part II focuses on computational approaches and tools used for identification, classification, and predictions of SH2 domain binding partners; Part III details various ways to prepare the SH2 domains as experimental reagents;

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Proteomic Clustering Analysis of SH2 Domain Datasetsode for processing data and preparing it for various types of analyses. Here I apply clustering analysis to previous collections of SH2 domains datasets to bring insight into new binding or specificity patterns between the different SH2 domains.

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NMR Chemical Shift Mapping of SH2 Peptide Interactionstein or to determine the binding affinity of a weak protein–peptide interaction. Here, we describe the application of NMR chemical shift mapping to the study of peptide binding to the C-terminal SH2 domain of PLCγ1.

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