E-Book

Intrinsically Disordered Proteins : Methods and Protocols [electronic resource]

  • Kragelund, Birthe B , Skriver, Karen. editor
  • Humana
  • 2020
Intrinsically Disordered Proteins : Methods and Protocols [electronic resource]
  • 자료유형
    단행본
  • 서명/저자사항
    Intrinsically Disordered Proteins :Methods and Protocols[electronic resource] / edited by Birthe B. Kragelund, Karen Skriver.
  • 판차
    1st ed. 2020.
  • 발행사항
    New York, NY : Humana, 2020.
  • 개인저자
    Kragelund, Birthe B, Skriver, Karen., editor
  • 단체저자
    SpringerLink (Online service)
  • 형태사항
    1 online resource.
  • 총서명
    Methods in Molecular Biology,1064-3745 ; 2141
  • 일반주제명
    Proteins.
    Protein Science
  • 기본자료 저록
    Springer Nature eBook
  • ISBN
    9781071605240
  • 언어
    영어

초록

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

목차

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-D횋COR: 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 Binding Reactions 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 A棺 Peptide and Setup of Reproducible Aggregation Kinetics Experiment
Measuring Interactions between Tau and Aggregation Inducers with Single Molecule F철rster 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 using Quantitative 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