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Intrinsically Disordered Proteins

Methods and Protocols

Specificaties
Gebonden, blz. | Engels
Springer US | e druk, 2020
ISBN13: 9781071605233
Rubricering
Springer US e druk, 2020 9781071605233
Onderdeel van serie Methods in Molecular Biology
€ 336,99
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Samenvatting

The edition details methods to study intrinsically disordered proteins (IDPs) including recent topics such as extremely high-affinity disordered complexes, kinetics that evade established concepts, liquid-liquid phase separation, and novel disorder-driven allosteric mechanisms. 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.

Authoritative and cutting-edge, Intrinsically Disordered Proteins: Methods and Protocols aims to help scientists with different backgrounds to further their investigations into these fascinating and dynamic molecules.

Chapter 24 is available open access under a CC BY 4.0 license via link.springer.com.

Chapters “40 and 42 ” are available open access under a Creative Commons Attribution 4.0 International License via link.springer.com.

Specificaties

ISBN13:9781071605233
Taal:Engels
Bindwijze:gebonden
Uitgever:Springer US

Inhoudsopgave

Disorder for Dummies: Functional Mutagenesis of Transient Helical Segments in Disordered Proteins.-&nbsp;Computational Prediction of Intrinsic Disorder in Protein Sequences with the disCoP Meta-predictor.-&nbsp;Computational Prediction of Disordered Protein Motifs using SLiMSuite.-&nbsp;How to Annotate and Submit a Short Linear Motif to the Eukaryotic Linear Motif Resource.-&nbsp;Analyzing the Sequences of Intrinsically Disordered Regions with CIDER and localCIDER.-&nbsp;Exploring Protein Intrinsic Disorder with MobiDB.-&nbsp;An Easy Protocol for Evolutionary Analysis of Intrinsically Disordered Proteins.-&nbsp;Expression and Purification of an Intrinsically Disordered Protein.-&nbsp;Production of Intrinsically Disordered Proteins for Biophysical Studies; Tips and Tricks.-&nbsp;Recombinant Production of Monomeric Isotope-Enriched Aggregation-Prone Peptides: Polyglutamine Tracts and Beyond.-&nbsp;Cell-free Protein Synthesis of Small Intrinsically Disordered Proteins for NMR Spectroscopy.-&nbsp;Structural Analyses of Intrinsically Disordered Proteins by Small-Angle X-ray Scattering.-&nbsp;Determining Rg of IDPs from SAXS data.-&nbsp;Obtaining Hydrodynamic Radii of Intrinsically Disordered Protein Ensembles by Pulsed Field Gradient NMR Measurements.-&nbsp;Quantitative Protein Disorder Assessment using NMR Chemical Shifts.-&nbsp;Determination of pK<sub>a</sub>&nbsp;Values in Intrinsically Disordered Proteins.-&nbsp;Paris-DÉCOR: A Protocol for the Determination of Fast Protein Backbone Amide Hydrogen Exchange Rates.-&nbsp;Predicting Conformational Properties of Intrinsically Disordered Proteins from Sequence.-&nbsp;Enhanced Molecular Dynamics Simulations of Intrinsically Disordered Proteins.-&nbsp;Computational Protocol for Determining Conformational Ensembles of Intrinsically Disordered Proteins.-&nbsp;Computing, Analyzing and Comparing the Radius of Gyration and Hydrodynamic Radius in Conformational Ensembles of Intrinsically Disordered Proteins.-&nbsp;Binding Thermodynamics to Intrinsically Disordered Protein Domains.-&nbsp;Analysis of Multivalent IDP Interactions: Stoichiometry, Affinity, and Local Concentration Effect Measurements.-&nbsp;NMR Lineshape Analysis of Intrinsically Disordered Protein Interactions.-&nbsp;Measuring Effective Concentrations Enforced by Intrinsically Disordered Linkers.-&nbsp;Determining the Protective Activity of IDPs under Partial Dehydration and Freeze-thaw Conditions.-&nbsp;Screening Intrinsically Disordered Regions for Short Linear Binding Motifs.-&nbsp;Probing IDP Interactions with Membranes by Fluorescence Spectroscopy.-&nbsp;Protocol for Investigating the Interactions between Intrinsically Disordered Proteins and Membranes by Neutron Reflectometry.-&nbsp;Interactions of IDPs with Membranes Using Dark State Exchange NMR Spectroscopy.-&nbsp;Determination of Binding Kinetics of Intrinsically Disordered Proteins by Surface Plasmon Resonance.-&nbsp;Measuring and Analysing Binding Kinetics of Coupled Folding and BindingReactions under Pseudo-first Order Conditions.-&nbsp;Understanding Binding Induced Folding by Temperature Jump.-&nbsp;Determining Binding Kinetics of Intrinsically Disordered Proteins by NMR spectroscopy.-&nbsp;Determination of Protein Phase Diagrams by Centrifugation.-&nbsp;In vitro&nbsp;Transition Temperature Measurement of Phase Separating Proteins by Microscopy.-&nbsp;Walking along a Protein Phase Diagram to Determine Coexistence Points by Static Light Scattering.-&nbsp;Expression and Purification of Intrinsically Disordered Aβ Peptide and Setup of Reproducible Aggregation Kinetics Experiment.-&nbsp;Measuring Interactions between Tau and Aggregation Inducers with Single Molecule Förster Resonance Energy Transfer.-&nbsp;Detection of Multisite Phosphorylation of Intrinsically Disordered Proteins using Phos-tag SDS-PAGE.-&nbsp;Multiple Site-specific Phosphorylation of IDPs Monitored by NMR.-&nbsp;Detection of Multisite Phosphorylation of Intrinsically Disordered Proteins usingQuantitative Mass-Spectrometry.-&nbsp;Targeting an Intrinsically Disordered Protein by Covalent Modification.-&nbsp;Recording in-cell NMR-spectra in Living Mammalian Cells.-&nbsp;In-cell NMR of Intrinsically Disordered Proteins in Mammalian Cells.-&nbsp;Analyzing IDPs in Interactomes.&nbsp;
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        Intrinsically Disordered Proteins