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| 008 | 171118s2018 xxu| s |||| 0|eng d | ||
| 020 | _a9781493973866 | ||
| 024 | 7 |
_a10.1007/978-1-4939-7386-6 _2doi |
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| 040 |
_aES-MaUEC _bspa _cES-MaUEC |
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| 245 | 1 | 0 |
_aProtein NMR _bMethods and Protocols _cedited by Ranajeet Ghose. |
| 250 | _a1st edition 2018 | ||
| 264 | 1 |
_aNew York, NY _bSpringer International Publishing _c2018 |
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| 300 |
_a1 recurso en línea (XIII, 446 páginas) _b62 ilustraciones a color |
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| 336 |
_atexto _btxt _2rdacontent |
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_aelectrónico _bc _2rdamedia |
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| 338 |
_arecurso electrónico _bcr _2rdacarrier |
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| 347 |
_aarchivo de texto _bPDF |
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| 490 | 0 |
_aMethods in Molecular Biology _x1940-6029 _v1688 |
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| 505 | 0 | _aNMR 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. . | |
| 520 | _aThis 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. | ||
| 700 | 1 |
_aGhose, Ranajeet _eeditor literario _4edt _4http://id.loc.gov/vocabulary/relators/edt |
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| 776 | 0 | 8 |
_iPrinted edition: _z9781493973859 |
| 776 | 0 | 8 |
_iPrinted edition: _z9781493973873 |
| 776 | 0 | 8 |
_iPrinted edition: _z9781493984695 |
| 856 | 4 | 0 |
_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1007/978-1-4939-7386-6 _z(usuarios Universidad Europea de Valencia) |
| 942 |
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| 988 | _aSpringer_Protocols_2018 | ||
| 999 |
_c233253 _d233253 |
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