Protein-protein interactions : methods and applications /
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Edition: | Second edition. |
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Imprint: | New York, NY : Humana Press, 2015. |
Description: | 1 online resource (xv, 620 pages) : illustrations (some color) |
Language: | English |
Series: | Methods in Molecular Biology, 1064-3745 ; 1278 Methods in molecular biology (Clifton, N.J.) ; v. 1278. |
Subject: | |
Format: | E-Resource Book |
URL for this record: | http://pi.lib.uchicago.edu/1001/cat/bib/11242452 |
Table of Contents:
- Structural basis of protein-protein interactions
- Quantitative analysis of protein-protein interactions
- Protein-protein interaction databases
- Computational prediction of protein-protein interactions.
- Structure-based computational approaches for small-molecule modulation of protein-protein interactions
- Targeting protein-protein interactions for drug discovery
- Studying protein-protein interactions using surface plasmon resonance
- Resonant waveguide grating for monitoring bimolecular interactions
- Quartz microbalance technology for probing biomolecular interactions
- Label-free kinetic analysis of an antibody-antigen interaction using biolayer interferometry
- Characterization of protein-protein interactions by isothermal titration calorimetry
- Sedimentation equilibrium studies
- Detecting protein-protein interactions by gel filtration chromatography
- Using light scattering to determine the stoichiometry of protein complexes
- Circular dichroism (CD) analyses of protein-protein interactions
- Protein-protein interaction analysis by nuclear magnetic resonance spectroscopy
- Quantitative protein analysis by mass spectrometry
- Using peptide arrays created by the SPOT method for defining protein-protein interactions
- Fluorescence polarization assay to quantify protein-protein interactions
- FoĢrster resonance energy transfer (FRET) microscopy for monitoring biomolecular interactions
- Utilizing ELISA to monitor protein-protein interactions
- Glutathione-S-transferase (GST)-fusion based assays for studying protein-protein interactions
- Hexahistidine (6xHis) fusion-based assays for protein-protein interactions
- Studying protein-protein interactions via blot overlay/Far Western blot
- Co-immunoprecipitation from transfected cells
- In vivo protein cross-linking
- Identification of protein-protein interactions by standard Gal4p-based yeast two-hybrid screening
- Reverse two-hybrid techniques in the yeast Saccharomyces cerevisiae
- MAPPIT, a mammalian two-hybrid method for in-cell detection of protein-protein interactions
- Bioluminescence resonance energy transfer to detect protein-protein interactions in live cells
- Mapping biochemical networks with protein fragment complementation assays
- Detection of protein-protein interaction using bimolecular fluorescence complementation assay
- Split-luciferase complementation assay to detect channel-protein interactions in live cells
- Confocal microscopy for intracellular co-localization of proteins
- Fluorescence polarization assay to quantify protein-protein interactions in an HTS format
- Estrogen receptor alpha/co-activator interaction assay
- TR-FRET
- High content screening biosensor assay to identify disruptors of p53-hDM2 protein-protein interactions
- Discovery of inhibitors of the MDM2-p53 protein-protein interaction
- Biophysical methods for identifying fragment-based inhibitors of protein-protein interactions.