Protein-ligand interactions : methods and applications /

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Bibliographic Details
Edition:	Third edition.
Imprint:	New York, NY : Humana Press, [2021]
Description:	1 online resource (xi, 492 pages) : illustrations (some color)
Language:	English
Series:	Methods in molecular biology, 1064-3745 Methods in molecular biology (Clifton, N.J.),
Subject:	Proteins -- Laboratory manuals. Ligands -- Laboratory manuals. Protein binding -- Laboratory manuals. Ligand binding (Biochemistry) -- Laboratory manuals. Ligand binding (Biochemistry) Ligands Protein binding Proteins Laboratory Manual Laboratory manuals Laboratory manuals.
Format:	E-Resource Book
URL for this record:	http://pi.lib.uchicago.edu/1001/cat/bib/12567710

Hidden Bibliographic Details
Other authors / contributors:	Daviter, Tina, editor. Johnson, Christopher M., editor. McLaughlin, Stephen H., editor. Williams, Mark A., Dr., editor.
ISBN:	9781071611975 1071611976 9781071611968
Notes:	Includes index. Online resource; title from PDF title page (SpringerLink, viewed April 27, 2021).
Summary:	This third edition provides new and updated chapters detailing a complete introduction to common and emerging procedures for characterizing the interactions of individual proteins with their natural ligands, drugs or other binding partners. Chapters detail natural substrates, potential drug leads, quantitative understanding of the mechanism of interaction, and different techniques. 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 accessible, Protein Ligand Interactions: Methods and Applications, Third Edition serves as an ideal guide for researchers new to the field of biophysical characterization of protein interactions.
Standard no.:	10.1007/978-1-0716-1197-5

Table of Contents:

Assessing and Improving Protein Sample Quality
A Familiar Protein-Ligand Interaction Revisited with Multiple Methods
Interactions of a Signal Transduction Protein Investigated by Fluorescence Stopped-Flow Kinetics
Kinetic Methods of Deducing Binding Mechanisms Involving Intrinsically Disordered Proteins
Isothermal Titration Calorimetry
Measuring the Kd of Protein-Ligand Interactions Using Microscale Thermophoresis
Quartz Crystal Microbalance with Dissipation Monitoring (QCM-D); Preparing Functionalized Lipid Layers for the Study of Complex Protein-Ligand Interactions
Indirect Detection of Ligand Binding by Thermal Melt Analysis
The Use of Acoustic Mist Ionization Mass Spectrometry for High-throughput Screening
Ligand Discovery
High Through-put Binding: Fluorescence Polarization (Anisotropy)
Fragment Screening by NMR
A Quick Primer in Fluorescence-based Equilibrium and Pre-Steady State Methods for Determining Protein-Nucleotide Affinities
Measurement of Nucleotide Hydrolysis using Fluorescent Biosensors for Phosphate
Gel-based Analysis of Protein-Nucleic Acid Interactions
Biophysical Studies of the Binding of Viral RNA with the 80S Ribosome using SwitchSENSE
Biolayer Interferometry: Protein-RNA Interactions
Analysis of Protein-DNA Interactions Using Surface Plasmon Resonance and a ReDCaT Chip
Characterization of Protein Nucleic Acid complexes by Size-Exclusion Chromatography Coupled with Light Scattering, Absorbance and Refractive Index Detectors
Analytical Ultracentrifugation for Analysis of Protein Nucleic Acid Interactions
Studying RNA-Protein Complexes Using X-ray Crystallography
Flow Linear Dichroism of Protein-membrane Systems
Probing Protein-Membrane Interactions and Dynamics Using Hydrogen-Deuterium eXchange Mass Spectrometry (HDX-MS).

Protein-ligand interactions : methods and applications /

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