Intrinsically Disordered Proteins

Exploring Protein Intrinsic Disorder with MobiDB

Seiten 127-143

Monzon, Alexander Miguel (et al.)

An Easy Protocol for Evolutionary Analysis of Intrinsically Disordered Proteins

Seiten 147-177

Nunez-Castilla, Janelle (et al.)

Expression and Purification of an Intrinsically Disordered Protein

Seiten 181-194

Singh, Karamjeet K. (et al.)

Production of Intrinsically Disordered Proteins for Biophysical Studies: Tips and Tricks

Seiten 195-209

Pedersen, Christian Parsbæk (et al.)

Recombinant Production of Monomeric Isotope-Enriched Aggregation-Prone Peptides: Polyglutamine Tracts and Beyond

Seiten 211-231

Escobedo, Albert (et al.)

Cell-Free Protein Synthesis of Small Intrinsically Disordered Proteins for NMR Spectroscopy

Seiten 233-245

Isaksson, Linnéa (et al.)

Structural Analyses of Intrinsically Disordered Proteins by Small-Angle X-Ray Scattering

Seiten 249-269

Sagar, Amin (et al.)

Determining Rg of IDPs from SAXS Data

Seiten 271-283

Rieloff, Ellen (et al.)

Obtaining Hydrodynamic Radii of Intrinsically Disordered Protein Ensembles by Pulsed Field Gradient NMR Measurements

Seiten 285-302

Leeb, Sarah (et al.)

Quantitative Protein Disorder Assessment Using NMR Chemical Shifts

Seiten 303-317

Nielsen, Jakob T. (et al.)

Determination of pKa Values in Intrinsically Disordered Proteins

Seiten 319-336

Payliss, Brandon (et al.)

Paris-DÉCOR: A Protocol for the Determination of Fast Protein Backbone Amide Hydrogen Exchange Rates

Seiten 337-344

Dass, Rupashree (et al.)

Predicting Conformational Properties of Intrinsically Disordered Proteins from Sequence

Seiten 347-389

Ruff, Kiersten M.

Enhanced Molecular Dynamics Simulations of Intrinsically Disordered Proteins

Seiten 391-411

Masetti, Matteo (et al.)

Computational Protocol for Determining Conformational Ensembles of Intrinsically Disordered Proteins

Seiten 413-427

Best, Robert B.

Computing, Analyzing, and Comparing the Radius of Gyration and Hydrodynamic Radius in Conformational Ensembles of Intrinsically Disordered Proteins

Seiten 429-445

Ahmed, Mustapha Carab (et al.)

Binding Thermodynamics to Intrinsically Disordered Protein Domains

Seiten 449-462

Schön, Arne (et al.)

Analysis of Multivalent IDP Interactions: Stoichiometry, Affinity, and Local Concentration Effect Measurements

Seiten 463-475

Sparks, Samuel (et al.)

NMR Lineshape Analysis of Intrinsically Disordered Protein Interactions

Seiten 477-504

Waudby, Christopher A. (et al.)

Measuring Effective Concentrations Enforced by Intrinsically Disordered Linkers

Seiten 505-518

Sørensen, Charlotte S. (et al.)

Determining the Protective Activity of IDPs Under Partial Dehydration and Freeze-Thaw Conditions

Seiten 519-528

Rendón-Luna, David F. (et al.)

Screening Intrinsically Disordered Regions for Short Linear Binding Motifs

Seiten 529-552

Ali, Muhammad (et al.)

Probing IDP Interactions with Membranes by Fluorescence Spectroscopy

Seiten 555-567

Acosta, Diana (et al.)

Protocol for Investigating the Interactions Between Intrinsically Disordered Proteins and Membranes by Neutron Reflectometry

Seiten 569-584

Luchini, Alessandra (et al.)

Interactions of IDPs with Membranes Using Dark-State Exchange NMR Spectroscopy

Seiten 585-608

Das, Tapojyoti (et al.)

Determination of Binding Kinetics of Intrinsically Disordered Proteins by Surface Plasmon Resonance

Seiten 611-627

Leth, Julie M. (et al.)

Measuring and Analyzing Binding Kinetics of Coupled Folding and Binding Reactions Under Pseudo-First-Order Conditions

Seiten 629-650

Jensen, Kristine Steen

Understanding Binding-Induced Folding by Temperature Jump

Seiten 651-661

Toto, Angelo (et al.)

Determining Binding Kinetics of Intrinsically Disordered Proteins by NMR Spectroscopy

Seiten 663-681

Yang, Ke (et al.)

Determination of Protein Phase Diagrams by Centrifugation

Seiten 685-702

Milkovic, Nicole M. (et al.)

In Vitro Transition Temperature Measurement of Phase-Separating Proteins by Microscopy

Seiten 703-714

Holland, Jack (et al.)

Walking Along a Protein Phase Diagram to Determine Coexistence Points by Static Light Scattering

Seiten 715-730

Peran, Ivan (et al.)

Expression and Purification of Intrinsically Disordered Aβ Peptide and Setup of Reproducible Aggregation Kinetics Experiment

Seiten 731-754

Linse, Sara

Measuring Interactions Between Tau and Aggregation Inducers with Single-Molecule Förster Resonance Energy Transfer

Seiten 755-775

Wickramasinghe, Sanjula P. (et al.)

Detection of Multisite Phosphorylation of Intrinsically Disordered Proteins Using Phos-tag SDS-PAGE

Seiten 779-792

Örd, Mihkel (et al.)

Multiple Site-Specific Phosphorylation of IDPs Monitored by NMR

Seiten 793-817

Julien, Manon (et al.)

Detection of Multisite Phosphorylation of Intrinsically Disordered Proteins Using Quantitative Mass-Spectrometry

Seiten 819-833

Valk, Ervin (et al.)

Targeting an Intrinsically Disordered Protein by Covalent Modification

Seiten 835-854

Nguyen, Hung Huy (et al.)

Recording In-Cell NMR-Spectra in Living Mammalian Cells

Seiten 857-871

Matečko-Burmann, Irena (et al.)

In-Cell NMR of Intrinsically Disordered Proteins in Mammalian Cells

Seiten 873-893

Gerez, Juan A. (et al.)

Analyzing IDPs in Interactomes

Seiten 895-945

Uversky, Vladimir N.