Protein NMR Spectroscopy : Principles and Practice. için kapak resmi
Protein NMR Spectroscopy : Principles and Practice.
Başlık:
Protein NMR Spectroscopy : Principles and Practice.
Yazar:
Cavanagh, John.
ISBN:
9780080471037
Yazar Ek Girişi:
Basım Bilgisi:
2nd ed.
Fiziksel Tanımlama:
1 online resource (915 pages)
İçerik:
Front cover -- Title page -- Copyright page -- Preface -- Preface to the First Edition -- Acknowledgements -- Table of Contents -- 1 Classical NMR Spectroscopy -- 1.1 Nuclear Magnetism -- 1.2 The Bloch Equations -- 1.3 The One-Pulse NMR Experiment -- 1.4 Linewidth -- 1.5 Chemical Shift -- 1.6 Scalar Coupling and Limitations of the Bloch Equations -- References -- 2 Theoretical Description of NMR Spectroscopy -- 2.1 Postulates of Quantum Mechanics -- 2.2 The Density Matrix -- 2.3 Pulses and Rotation Operators -- 2.4 Quantum Mechanical NMR Spectroscopy -- 2.5 Quantum Mechanics of Multispin Systems -- 2.6 Coherence -- 2.7 Product Operator Formalism -- 2.8 Averaging of the Spin Hamiltonians and Residual Interactions -- References -- 3 Experimental Aspects of NMR Spectroscopy -- 3.1 NMR Instrumentation -- 3.2 Data Acquisition -- 3.3 Data Processing -- 3.4 Pulse Techniques -- 3.5 Spin Decoupling -- 3.6 B0 Field Gradients -- 3.7 Water Suppression Techniques -- 3.8 One-Dimensional 1H NMR Spectroscopy -- References -- 4 Multidimensional NMR Spectroscopy -- 4.1 Two-Dimensional NMR Spectroscopy -- 4.2 Coherence Transfer and Mixing -- 4.3 Coherence Selection, Phase Cycling, and Field Gradients -- 4.4 Resolution and Sensitivity -- 4.5 Three- and Four-Dimensional NMR Spectroscopy -- References -- 5 Relaxation and Dynamic Processes -- 5.1 Introduction and Survey of Theoretical Approaches -- 5.2 The Master Equation -- 5.3 Spectral Density Functions -- 5.4 Relaxation Mechanisms -- 5.5 Nuclear Overhauser Effect -- 5.6 Chemical Exchange Effects in NMR Spectroscopy -- References -- 6 Experimental 1H NMR Methods -- 6.1 Assessment of the 1D 1H Spectrum -- 6.2 COSY-Type Experiments -- 6.3 Multiple-Quantum Filtered COSY -- 6.4 Multiple-Quantum Spectroscopy -- 6.5 TOCSY -- 6.6 Cross-Relaxation NMR Experiments -- 6.7 1H 3D Experiments -- References.

7 Heteronuclear NMR Experiments -- 7.1 Heteronuclear Correlation NMR Spectroscopy -- 7.2 Heteronuclear-Edited NMR Spectroscopy -- 7.3 13C-13C Correlations: The HCCH-COSY and HCCH-TOCSY Experiments -- 7.4 3D Triple-Resonance Experiments -- 7.5 Measurement of Scalar Coupling Constants -- 7.6 Measurement of Residual Dipolar Coupling Constants -- References -- 8 Experimental NMR Relaxation Methods -- 8.1 Pulse Sequences and Experimental Methods -- 8.2 Picosecond-Nanosecond Dynamics -- 8.3 Microsecond-Second Dynamics -- References -- 9 Larger Proteins and Molecular Interactions -- 9.1 Larger Proteins -- 9.2 Intermolecular Interactions -- 9.3 Methods for Rapid Data Acquisition -- References -- 10 Sequential Assignment, Structure Determination, and Other Applications -- 10.1 Resonance Assignment Strategies -- 10.2 Three-Dimensional Solution Structures -- 10.3 Conclusion -- References -- Table of Symbols -- List of Figures -- List of Tables -- Suggested Reading -- Biomolecular NMR Spectroscopy -- NMR Spectroscopy -- Quantum Mechanics -- Index -- Spin-1/2 Product Operator Equations -- Table of Constants.
Özet:
Protein NMR Spectroscopy combines a comprehensive theoretical treatment of NMR spectroscopy with an extensive exposition of the experimental techniques applicable to proteins and other biological macromolecules in solution. Beginning with simple theoretical models and experimental techniques, Protein NMR Spectroscopy develops the complete repertoire of theoretical principles and experimental techniques necessary for understanding and implementing the most sophisticated NMR experiments. Important new techniques and applications of NMR spectroscopy have emerged since the first edition of this extremely successful book was published in 1996. The second edition includes new sections describing measurement and use of residual dipolar coupling constants for structure determination, TROSY and deuterium labeling for application to large macromolecules, and experimental techniques for characterizing conformational dynamics. In addition, the treatments of instrumentation and signal acquisition, field gradients, multidimensional spectroscopy, and structure calculation are updated and enhanced. Protein NMR Spectroscopy is written as a graduate-level textbook and will be of interest to biochemists, chemists, biophysicists, and structural biologists who utilize NMR spectroscopy or who wish to understand the latest developments in this field. · Provides an understanding of the theoretical principles important for biological NMR spectroscopy · Demonstrates how to implement, optimize and troubleshoot modern multi-dimensional NMR experiments · Allows for the capability of designing effective experimental protocols for investigations of protein structures and dynamics · Includes a comprehensive set of example NMR spectra of ubiquitin provides a reference for validation of experimental methods.
Notlar:
Electronic reproduction. Ann Arbor, Michigan : ProQuest Ebook Central, 2017. Available via World Wide Web. Access may be limited to ProQuest Ebook Central affiliated libraries.
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