Protein Self-Assembly [E-Book] : Methods and Protocols / edited by Jennifer J. McManus.
McManus, Jennifer J., (editor)
1st edition 2019.
New York, NY : Humana Press, 2019
X, 266 pages 87 illustrations, 59 illustrations in color (online resource)
englisch
9781493996780
10.1007/978-1-4939-9678-0
Methods in Molecular Biology ; 2039
Full Text
Table of Contents:
  • Measuring Non-Specific Protein-Protein Interactions by Dynamic Light Scattering
  • Light Scattering to Quantify Protein-Protein Interactions at High Protein Concentrations
  • Quantitative Evaluation of Protein Solubility in Aqueous Solutions by PEG-Induced Liquid-Liquid Phase Separation
  • Measuring Protein Solubility
  • Integral caa3-Cytochrome c Oxidase from Thermus thermophiles: Purification and Crystallization
  • Aggregation Profiling of C9orf72 Dipeptide Repeat Proteins Transgenically Expressed in Drosophila melanogaster using an Analytical Ultracentrifuge Equipped with Fluorescence Detection
  • Sample Preparation and Size Analysis of C9orf72 Dipeptide Repeat Proteins Expressed in Drosophila melanogaster using Semi-Denaturing Agarose Gel Electrophoresis
  • The Use of High Performance Liquid Chromatography for the Characterization of the Unfolding and Aggregation of Dairy Proteins
  • Differential Scanning Calorimetry to Quantify Heat Induced Aggregation in Concentrated Protein Solution
  • Nanoparticle Tracking Analysis to Examine the Temperature-Induced Aggregation of Proteins
  • Evaluation of Temporal Aggregation Processes using Spatial Intensity Distribution Analysis
  • Fluorescence Correlation Spectroscopy for Particle Sizing in Highly Concentrated Protein Solutions
  • Size Determination of Protein Oligomers/Aggregates Using Diffusion NMR Spectroscopy
  • Patchy Particle models to Understand Protein Phase Behavior
  • Obtaining Soft Matter Models of Proteins and their Phase Behavior
  • Binding Free Energies of Conformationally Disordered Peptides through Extensive Sampling and End-Point Methods
  • Atomistic Simulation Tools to Study Protein Self-Aggregation.