Lipid-Protein Interactions -

Lipid-Protein Interactions

Methods and Protocols

Jörg H. Kleinschmidt (Herausgeber)

Buch | Hardcover
682 Seiten
2019 | 2nd ed. 2019
Humana Press Inc. (Verlag)
978-1-4939-9511-0 (ISBN)
246,09 inkl. MwSt
This second edition volume expands all chapters of the previous edition, which have been enhanced to cover the most recent developments, the current state of method research, and applications. Additional protocols were added to examine lipid-protein interactions by mass spectrometry, to use protein microarrays to investigate large sets of various proteins, to study membrane protein dynamics by UV resonance Raman spectroscopy, to analyze peptide-induced pore formation in membranes, and to investigate folding and insertion of membrane proteins. 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.

Cutting-edge and authoritative, Lipid-Protein Interactions: Methods and Protocols, Second Edition is an essential resource for all researchers who are interested in obtaining up-to-date and comprehensive information about membrane structure and function.

Multiscale Modeling and Simulation Approaches to Lipid-Protein Interactions.- Quartz Crystal Microbalances as Tools for Probing Protein-Membrane Interactions.- Surface Plasmon Resonance for Measuring Interactions of Proteins with Lipids and Lipid Membranes.- Thermodynamic Analysis of Protein-Lipid Interactions by Isothermal Titration Calorimetry.- Differential Scanning Calorimetry of Protein-Lipid Interactions.- Imaging and Force Spectroscopy of Single Transmembrane Proteins with the Atomic Force Microscope.- Kinetics of Insertion and Folding of Outer Membrane Proteins by Gel-Electrophoresis.- Optimized Negative-Staining Protocol for Lipid-Protein Interactions Investigated by Electron Microscopy.- Probing Heterogeneous Lipid Interactions with Membrane Proteins using Mass Spectrometry.- Protein Microarrays and Liposome: A Method for Studying Lipid-Protein Interactions.- Structural Investigations of Protein-Lipid Complexes using Neutron Scattering.- Circular-Dichroism and Synchrotron-Radiation Circular-Dichroism Spectroscopy as Tools to Monitor Protein Structure in a Lipid Environment.- FTIR Analysis of Proteins and Protein-Membrane Interactions.- UV Resonance Raman Spectroscopy as a Tool to Probe Membrane Protein Structure and Dynamics.- Analyzing Transmembrane Protein and Hydrophobic Helix Topography by Dual Fluorescence Quenching.- Förster Resonance Energy Transfer as a Tool for Quantification of Protein-Lipid Selectivity.- A Guide to Tracking Single Membrane Proteins and Their Interactions in Supported Lipid Bilayers.- Fluorescence Correlation Spectroscopy to Examine Protein-Lipid Interactions in Membranes.- Membrane Pore Formation by Peptides Studied by Fluorescence Techniques.- Folding and Insertion of β-Barrel Membrane Proteins into Lipid Membranes by Site-Directed Fluorescence Spectroscopy.- EPR Techniques to Probe Insertion and Conformation of Spin-Labeled Proteins inLipid Bilayers.- Studying Lipid-Protein Interactions with Electron Paramagnetic Resonance Spectroscopy of Spin-Labeled Lipids.- Solid-State NMR Approaches to Study Protein Structure and Protein-Lipid Interactions.- Solution NMR Spectroscopy for the Determination of Structures of Membrane Proteins in Lipid Environment.- Nanodiscs as a New Tool to Examine Lipid-Protein Interactions.

Erscheinungsdatum
Reihe/Serie Methods in Molecular Biology ; 2003
Zusatzinfo 92 Illustrations, color; 55 Illustrations, black and white; XIV, 682 p. 147 illus., 92 illus. in color.
Verlagsort Totowa, NJ
Sprache englisch
Maße 178 x 254 mm
Themenwelt Naturwissenschaften Biologie Biochemie
Naturwissenschaften Biologie Mikrobiologie / Immunologie
Naturwissenschaften Chemie Analytische Chemie
ISBN-10 1-4939-9511-1 / 1493995111
ISBN-13 978-1-4939-9511-0 / 9781493995110
Zustand Neuware
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