Intrinsically Disordered Proteins Methods and Protocols /
| Corporate Author: | |
|---|---|
| Other Authors: | , |
| Summary: | XVIII, 951 p. 231 illus., 192 illus. in color. text |
| Language: | English |
| Published: |
New York, NY :
Springer US : Imprint: Humana,
2020.
|
| Edition: | 1st ed. 2020. |
| Series: | Methods in Molecular Biology,
2141 |
| Subjects: | |
| Online Access: | https://doi.org/10.1007/978-1-0716-0524-0 |
| Format: | Electronic eBook |
Table of Contents:
- Disorder for Dummies: Functional Mutagenesis of Transient Helical Segments in Disordered Proteins
- Computational Prediction of Intrinsic Disorder in Protein Sequences with the disCoP Meta-predictor
- Computational Prediction of Disordered Protein Motifs using SLiMSuite
- How to Annotate and Submit a Short Linear Motif to the Eukaryotic Linear Motif Resource
- Analyzing the Sequences of Intrinsically Disordered Regions with CIDER and localCIDER
- Exploring Protein Intrinsic Disorder with MobiDB
- An Easy Protocol for Evolutionary Analysis of Intrinsically Disordered Proteins
- Expression and Purification of an Intrinsically Disordered Protein
- Production of Intrinsically Disordered Proteins for Biophysical Studies; Tips and Tricks
- Recombinant Production of Monomeric Isotope-Enriched Aggregation-Prone Peptides: Polyglutamine Tracts and Beyond
- Cell-free Protein Synthesis of Small Intrinsically Disordered Proteins for NMR Spectroscopy
- Structural Analyses of Intrinsically Disordered Proteins by Small-Angle X-ray Scattering
- Determining Rg of IDPs from SAXS data
- Obtaining Hydrodynamic Radii of Intrinsically Disordered Protein Ensembles by Pulsed Field Gradient NMR Measurements
- Quantitative Protein Disorder Assessment using NMR Chemical Shifts
- Determination of pKa Values in Intrinsically Disordered Proteins
- Paris-DÉCOR: A Protocol for the Determination of Fast Protein Backbone Amide Hydrogen Exchange Rates
- Predicting Conformational Properties of Intrinsically Disordered Proteins from Sequence
- Enhanced Molecular Dynamics Simulations of Intrinsically Disordered Proteins
- Computational Protocol for Determining Conformational Ensembles of Intrinsically Disordered Proteins
- Computing, Analyzing and Comparing the Radius of Gyration and Hydrodynamic Radius in Conformational Ensembles of Intrinsically Disordered Proteins
- Binding Thermodynamics to Intrinsically Disordered Protein Domains
- Analysis of Multivalent IDP Interactions: Stoichiometry, Affinity, and Local Concentration Effect Measurements
- NMR Lineshape Analysis of Intrinsically Disordered Protein Interactions
- Measuring Effective Concentrations Enforced by Intrinsically Disordered Linkers
- Determining the Protective Activity of IDPs under Partial Dehydration and Freeze-thaw Conditions
- Screening Intrinsically Disordered Regions for Short Linear Binding Motifs
- Probing IDP Interactions with Membranes by Fluorescence Spectroscopy
- Protocol for Investigating the Interactions between Intrinsically Disordered Proteins and Membranes by Neutron Reflectometry
- Interactions of IDPs with Membranes Using Dark State Exchange NMR Spectroscopy
- Determination of Binding Kinetics of Intrinsically Disordered Proteins by Surface Plasmon Resonance
- Measuring and Analysing Binding Kinetics of Coupled Folding and BindingReactions under Pseudo-first Order Conditions
- Understanding Binding Induced Folding by Temperature Jump
- Determining Binding Kinetics of Intrinsically Disordered Proteins by NMR spectroscopy
- Determination of Protein Phase Diagrams by Centrifugation
- In vitro Transition Temperature Measurement of Phase Separating Proteins by Microscopy
- Walking along a Protein Phase Diagram to Determine Coexistence Points by Static Light Scattering
- Expression and Purification of Intrinsically Disordered Aβ Peptide and Setup of Reproducible Aggregation Kinetics Experiment
- Measuring Interactions between Tau and Aggregation Inducers with Single Molecule Förster Resonance Energy Transfer
- Detection of Multisite Phosphorylation of Intrinsically Disordered Proteins using Phos-tag SDS-PAGE
- Multiple Site-specific Phosphorylation of IDPs Monitored by NMR
- Detection of Multisite Phosphorylation of Intrinsically Disordered Proteins usingQuantitative Mass-Spectrometry
- Targeting an Intrinsically Disordered Protein by Covalent Modification
- Recording in-cell NMR-spectra in Living Mammalian Cells
- In-cell NMR of Intrinsically Disordered Proteins in Mammalian Cells
- Analyzing IDPs in Interactomes. .