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Nuclear magnetic resonance of biological macromolecules : Pt. C / ed. by Thomas L. James

The critically acclaimed laboratory standard, Methods in Enzymology, is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. The series contains much materia... Full description

PPN (Catalogue-ID): 549068635
Personen: James, Thomas L.
Format: eBook eBook
Enthält: Cover; Copyright Page; Table of Contents; Contributors to Volume 394; Volumes in Series; Section I: Techniques: Spectral, Experimental, and Analytical; Chapter 1. Identification and Optimization of Protein Domains for NMR Studies; Chapter 2. In-Cell NMR Spectroscopy; Chapter 3. Molecular Fragment Replacement Approach to Protein Structure Determination by Chemical Shift and Dipolar Homology Database Mining; Chapter 4. Rapid NMR Data Collection; Section II: Proteomics; Chapter 5. An Integrated Platform for Automated Analysis of Protein NMR Structures
Language: English
Published: Amsterdam [u.a.], Elsevier, 2005
Series: Methods in enzymology (394)
Basisklassifikation: 35.25
35.71
35.75
35.76
44.64
Notes: Literaturangaben
Physical Description: Online-Ressource (XXXVII, 631, [34] S.)
Enthaltenes Werk
Gesamtaufnahme:
Zur Gesamtaufnahme , Pt. C
Link: Inhaltsverzeichnis
ISBN: 0-12-182799-2
978-0-12-182799-1
Sekundärausgabe Online-Ausg., 2009

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245 1 0 |a Nuclear magnetic resonance of biological macromolecules  |n Pt. C  |c ed. by Thomas L. James 
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490 1 |a Methods in enzymology  |v 394 
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501 |a Cover; Copyright Page; Table of Contents; Contributors to Volume 394; Volumes in Series; Section I: Techniques: Spectral, Experimental, and Analytical; Chapter 1. Identification and Optimization of Protein Domains for NMR Studies; Chapter 2. In-Cell NMR Spectroscopy; Chapter 3. Molecular Fragment Replacement Approach to Protein Structure Determination by Chemical Shift and Dipolar Homology Database Mining; Chapter 4. Rapid NMR Data Collection; Section II: Proteomics; Chapter 5. An Integrated Platform for Automated Analysis of Protein NMR Structures 
501 |a Chapter 6. Rapid Assessment of Protein Structural Stability and Fold Validation via NMRChapter 7. Determination of Protein Backbone Structures from Residual Dipolar Couplings; Chapter 8. Robotic Cloning and Protein Production Platform of the Northeast Structural Genomics Consortium; Chapter 9. Protein Structure Estimation from Minimal Restraints Using Rosetta; Chapter 10. Protein Structure Elucidation from Minimal NMR Data: The CLOUDS Approach; Section III: Challenging Systems for NMR; Chapter 11. Elucidation of the Protein Folding Landscape by NMR 
501 |a Chapter 12. Membrane Protein Preparation for TROSY NMR ScreeningChapter 13. Solution Structure and Dynamics of Integral Membrane Proteins by NMR: A Case Study Involving the Enzyme PagP; Chapter 14. NMR Experiments on Aligned Samples of Membrane Proteins; Chapter 15. NMR Techniques Used with Very Large Biological Macromolecules in Solution; Chapter 16. Structure Determination of Large Biological RNAs; Section IV: Macromolecular Dynamics; Chapter 17. Hydrodynamic Models and Computational Methods for NMR Relaxation 
501 |a Chapter 18. Solution NMR Spin Relaxation Methods for Characterizing Chemical Exchange in High-Molecular-Weight SystemsChapter 19. Isotropic Reorientational Eigenmode Dynamics Complements NMR Relaxation Measurements for RNA; Section V: Macromolecular Complexes; Chapter 20. NMR Techniques for Identifying the Interface of a Larger Protein-Protein Complex: Cross-Saturation and Transferred Cross-Saturation Experiments; Chapter 21. Enzyme Dynamics During Catalysis Measured by NMR Spectroscopy; Chapter 22. Structure Determination of Protein/RNA Complexes by NMR; Section VI: Ligand Discovery 
501 |a Chapter 23. Utilization of NMR-Derived Fragment Leads in Drug DesignChapter 24. Discovery of Ligands by a Combination of Computational and NMR-Based Screening: RNA as an Example Target; Author Index; Subject Index 
520 |a The critically acclaimed laboratory standard, Methods in Enzymology, is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. The series contains much material still relevant today - truly an essential publication for researchers in all fields of life sciences. Nuclear Magnetic Resonance of Biological Macromolecules, Part C is written with a hands-on perspective. That is, practical applications with critical evaluations of methodologies and experimental considerations needed to design, execute, and interpret NMR experiments pertinent to biological molecules. * One of the most highly respected publications in the field of biochemistry since 1955 * Frequently consulted, and praised by researchers and reviewers alike * Truly an essential publication for anyone in any field of the life sciences 
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