Intrinsically Disordered Protein Analysis

Volume 2, Methods and Experimental Tools

AvVladimir N. Uversky,A. Keith Dunker

Häftad, Engelska, 2016

Del 896 i serien Methods in Molecular Biology

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Beskrivning

Over the past decade, there has been an explosive development of research of intrinsically disordered proteins (IDPs), which are also known as unfolded proteins.

Produktinformation

Utgivningsdatum:2016-08-23
Mått:178 x 254 x 26 mm
Vikt:873 g
Format:Häftad
Språk:Engelska
Serie:Methods in Molecular Biology
Antal sidor:454
Förlag:Springer-Verlag New York Inc.
ISBN:9781493944842

Utforska kategorier

Biokemi inom Naturvetenskap och teknik

Innehållsförteckning

Immobilization of Proteins for Single Molecule Fluorescence Resonance Energy Transfer Measurements of Conformation and Dynamics.-Application of Confocal Single Molecule FRET to Intrinsically Disordered Proteins.-Single-Molecule Force Spectroscopy of Chimeric Polyprotein Constructs Containing Intrinsically Disordered Domains.-Visualization of Mobility by Atomic Force Microscopy.-Unequivocal Single-Molecule Force Spectroscopy of Intrinsically Disordered Proteins.-Sedimentation Velocity Analytical Ultracentrifugation for Intrinsically Disordered Proteins.-Analysis of Intrinsically Disordered Proteins by Small-Angle X-ray Scattering.-Small Angle Neutron Scattering (SANS) for the Structural Study of Intrinsically Disordered Proteins in Solution: a Practical Guide.-Dynamic and Static Light Scattering of Intrinsically Disordered Proteins.-Estimation of Intrinsically Disordered Protein Shape and Time-averaged Apparent Hydration in Native Conditions by a Combination of Hydrodynamic Methods.-Size-Exclusion Chromatography in Structural Analysis of Intrinsically Disordered Proteins.-Denaturant-induced Conformational Transitions in Intrinsically Disordered Proteins.-Identification of Intrinsically Disordered Proteins by a Special 2D Electrophoresis.-pH-induced Changes in Intrinsically-disordered Proteins.-Temperature Induced Transitions in Disordered Proteins Probed by NMR Spectroscopy.-Analyzing Temperature Induced Transitions in Disordered Proteins by NMR Spectroscopy and Secondary Chemical Shift Analyses.-Osmolyte-, Binding-, and Temperature-Induced Transitions of Intrinsically Disordered Proteins.-Laser Temperature-jump Spectroscopy of Intrinsically Disordered Proteins.-Differential Scanning Microcalorimetry of Intrinsically Disordered Proteins.-Identifying Disordered Regions in Proteins by Limited Proteolysis.-The Effect of Counter Ions on the Conformation of Intrinsically Disordered Proteins Studied by Size-exclusion Chromatography.-Mean Net Charge of Intrinsically Disordered Proteins: Experimental Determination of Protein Valence by Electrophoretic Mobility Measurements.-Protein Characterization by Partitioning in Aqueous Two-Phase Systems.-Detection and Characterization of Large-scale Protein Conformational Transitions in Solution using Charge-state Distribution Analysis in ESI-MS.-Localizing Flexible Regions in Proteins using Hydrogen Deuterium Exchange Mass Spectrometry.-Mass-spectrometry Tools for Analysis of Intermolecular Interactions.-Characterization of Oligomerization- Aggregation Products of Neurodegenerative Target Proteins by Ion Mobility Mass Spectrometry.-Identifying Solubility-promoting Buffers for Intrinsically Disordered Proteins Prior to Purification.-Proteomic Methods for the Identification of Intrinsically Disordered Proteins.-Selective Isotope Labeling of Recombinant Proteins in E. coli.