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Protein-Ligand Interactions: Methods and Applications Third Edition 2021 [Minkštas viršelis]

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  • Formatas: Paperback / softback, 492 pages, aukštis x plotis: 254x178 mm, weight: 950 g, 80 Illustrations, color; 43 Illustrations, black and white; XI, 492 p. 123 illus., 80 illus. in color., 1 Paperback / softback
  • Serija: Methods in Molecular Biology 2263
  • Išleidimo metai: 21-Apr-2021
  • Leidėjas: Springer-Verlag New York Inc.
  • ISBN-10: 1071611992
  • ISBN-13: 9781071611999
Kitos knygos pagal šią temą:
Protein-Ligand Interactions: Methods and Applications Third Edition 2021Didesnis paveikslėlis
  • Formatas: Paperback / softback, 492 pages, aukštis x plotis: 254x178 mm, weight: 950 g, 80 Illustrations, color; 43 Illustrations, black and white; XI, 492 p. 123 illus., 80 illus. in color., 1 Paperback / softback
  • Serija: Methods in Molecular Biology 2263
  • Išleidimo metai: 21-Apr-2021
  • Leidėjas: Springer-Verlag New York Inc.
  • ISBN-10: 1071611992
  • ISBN-13: 9781071611999
Kitos knygos pagal šią temą:
Pastovi nuoroda: https://www.kriso.lt/db/9781071611999.html
Raktažodžiai:
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.
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).