Buch, Englisch, Band 2705, 382 Seiten, Format (B × H): 178 mm x 254 mm, Gewicht: 742 g
Reihe: Methods in Molecular Biology
Functional Modules and Evolving Tools in Biology
Buch, Englisch, Band 2705, 382 Seiten, Format (B × H): 178 mm x 254 mm, Gewicht: 742 g
Reihe: Methods in Molecular Biology
ISBN: 978-1-0716-3395-3
Verlag: Springer
This volume looks at the latest methods used to study and modulate the biological function and mechanisms of SH2 domains. The chapters in this book are organized into five parts. Part One presents methodology aimed at determining the structures and dynamics of SH2 domains and their complexes with phosphopeptides. Part Two discusses techniques to understand and predict interactions of SH2 domains by measuring or calculating their affinity to phosphopeptides. Part Three focuses on inhibitors of SH2 domains that lead the way for chemical tool development and drug discovery. Part Four describes how to evolve and engineer SH2 domains with specific binding properties, and Part Five explores how to measure the regulation of protein tyrosine phosphatase activity through allosteric binding of peptides to SH2 domains and condensation. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls.
Cutting-edge and comprehensive, SH2 Domains: Functional Modules and Evolving Tools in Biology is a valuable resource for researchers, working in the biophysical and biochemical field, who want to learn more about this exciting and versatile class of regulatory and signaling domains.
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Weitere Infos & Material
Methods for Structure Determination of SH2 Domain–Phosphopeptide Complexes by NMR.- NMR Methods to Study the Dynamics of SH2 Domain–Phosphopeptide Complexes.- Crystal Structure Analysis of SH2 Domains in Complex with Phosphotyrosine Peptides.- Revealing Allostery in PTPN11 SH2 Domains from MD Simulations.- Structure Determination of SH2–Phosphopeptide Complexes by X-Ray Crystallography: The Example of p120RasGAP.- Fluorescence Anisotropy and Polarization in the Characterization of Biomolecular Association Processes and Their Application to Study SH2 Domain Binding Affinity.- Computational Evaluation of Peptide-Protein Binding Affinities: Application of Potential of Mean Force Calculations to SH2 Domains.- NMR Relaxation Dispersion Experiments to Study Phosphopeptide Recognition by SH2 Domains: The Grb2-SH2–Phosphopeptide Encounter Complex.- Using Linear Motif Database Resources to Identify SH2 Domain Binders.- Using Surface Plasmon Resonance to Study SH2 Domain-Peptide Interactions.- Inhibitor Library Screening of SH2 Domains through Denaturation-Based Assays.- Dissecting Selectivity Determinants of Small-Molecule Inhibitors of SH2-Domains via Fluorescence Polarization Assays.- Lipid Binding of SH2 Domains.- Exploring the Binding Interaction between Phosphotyrosine Peptides and SH2 Domains by Proximal Crosslinking.- Synthesis and Biochemical Evaluation of Monocarboxylic GRB2 SH2 Domain Inhibitors.- Engineering of SH2 Domains for the Recognition of Protein Tyrosine O-Sulfation Sites.- Engineering SH2 Domains with Tailored Specificities and Affinities.- Measuring Protein Tyrosine Phosphatase Activity Dependent on SH2 Domain-Mediated Regulation.- Peptides as Baits for the Co-Precipitation of SH2 Domain-Containing Proteins.- Biomolecular Condensation of SH2 Domain-Containing Proteins on Membranes.
