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Protein NMR: Methods and Protocols Softcover reprint of the original 1st ed. 2018 [Pehme köide]

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  • Formaat: Paperback / softback, 446 pages, kõrgus x laius: 254x178 mm, kaal: 868 g, 62 Illustrations, color; XIII, 446 p. 62 illus. in color., 1 Paperback / softback
  • Sari: Methods in Molecular Biology 1688
  • Ilmumisaeg: 23-May-2018
  • Kirjastus: Humana Press Inc.
  • ISBN-10: 1493984691
  • ISBN-13: 9781493984695
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Protein NMR: Methods and Protocols Softcover reprint of the original 1st ed. 2018Suurem pilt
  • Formaat: Paperback / softback, 446 pages, kõrgus x laius: 254x178 mm, kaal: 868 g, 62 Illustrations, color; XIII, 446 p. 62 illus. in color., 1 Paperback / softback
  • Sari: Methods in Molecular Biology 1688
  • Ilmumisaeg: 23-May-2018
  • Kirjastus: Humana Press Inc.
  • ISBN-10: 1493984691
  • ISBN-13: 9781493984695
Teised raamatud teemal:
Püsilink: https://www.kriso.ee/db/9781493984695.html

This volume covers state-of-the-art applications of solid-state and solution nuclear magnetic resonance( NMR) spectroscopy to study protein structure, dynamics and interactions. Chapters detail various aspects of data acquisition and processing, determination of the structure, multi-timescale dynamics of entities ranging from individual proteins to large macromolecular complexes to intact viral assemblies. The final two chapters will highlight the promise of NMR beyond field strengths of 1 GHz to study the structure, dynamics and interactions of a larger class of proteins and protein complexes of extraordinary biological interest.  Written in the highly successful Methods in Molecular Biology series format, chapters provide detailed laboratory protocols and troubleshooting tips that would be of great practical help to NMR spectroscopists with different levels of expertise.

Authoritative and cutting-edge, Protein NMR: Methods and Protocol aims to ensure successful results in the further study of this vital field.

Arvustused

The book covers current applications of solid-state and solution nuclear magnetic resonance spectroscopy to study protein structure, dynamics. and interactions. Written in the highly successful Methods in Molecular Biology series format, chapters provide detailed laboratory protocols with tips to tackle troubleshooting. The book has several high quality illustrations in color or black and white. The intended audience appears to be students, specialists, and those who are interested in NMR spectroscopy. (Omer Iqbal, Doody's Book Reviews, April, 2018)

NMR of Macromolecular Assemblies and Machines at 1 GHz and Beyond: New
Transformative Opportunities for Molecular Structural Biology.- Experimental
Aspects of Polarization Optimized Experiments (POE) for Magic Angle Spinning
Solid-state NMR of Microcrystalline and Membrane-Bound Proteins.- Afterglow
Solid-State NMR Spectroscopy.- Filamentous Bacteriophage Viruses:
Preparation, Magic-angle Spinning Solid-state NMR Experiments and Structure
Determination.- Spherical Nanoparticle Supported Lipid Bilayers: A Tool for
Modeling Protein Interactions with Curved Membranes.- Rapid Prediction of
Multi-dimensional NMR Data Sets using FANDAS.- Strategies for Efficient
Sample Preparation for Dynamic Nuclear Polar­ization Solid State NMR of
Biological Macromolecules.- In-vitro Dissolution Dynamic Nuclear Polarization
for Sensitivity Enhancement of NMR with Biological Molecules.- Determination
of Protein ps-ns Motions by High-Resolution Relaxometry.- Characterizing
Protein Dynamics with NMR R1r Relaxation Experiments.- CPMG Experiments for
Protein Minor Conformer Structure Determination.- Probing the Atomic
Structure of Transient Protein Contacts by Paramagnetic Relaxation
Enhancement Solution NMR.- From Raw Data to Protein Backbone Chemical Shifts
Using NMRFx Processing and NMRViewJ Analysis.- Protein Structure Elucidation
from NMR Data with the Program Xplor-NIH.- Practical Nonuniform Sampling and
Non-Fourier Spectral Reconstruction for Multidimensional NMR.- Covariance NMR
Processing and Analysis for Protein Assignment.- Structures of Dynamic
Protein Complexes: Hybrid Techniques to Study MAP Kinase Complexes and the
ESCRT System.- Implementation of the NMR CHEmical Shift Covariance Analysis
(CHESCA): A Chemical Biologists Approach to Allostery.- High-efficiency
Expression of Yeast-derived G Protein-coupled Receptors and 19F Labeling for
Dynamical Studies.- Quantitative Determination of Interacting Protein
Surfaces in Prokaryotes and Eukaryotes by Using In-cell NMR Spectroscopy.