Ghose | Protein NMR | Buch | 978-1-4939-7385-9 | sack.de

Buch, Englisch, Band 1688, 446 Seiten, HC runder Rücken kaschiert, Format (B × H): 183 mm x 260 mm, Gewicht: 10025 g

Reihe: Methods in Molecular Biology

Ghose

Protein NMR

Methods and Protocols

Buch, Englisch, Band 1688, 446 Seiten, HC runder Rücken kaschiert, Format (B × H): 183 mm x 260 mm, Gewicht: 10025 g

Reihe: Methods in Molecular Biology

ISBN: 978-1-4939-7385-9
Verlag: Springer


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.
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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 Biologist’s 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.


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