Fundamentals of Protein NMR Spectroscopy

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Oktober 2005



NMR spectroscopy has proven to be a powerful technique to study the structure and dynamics of biological macromolecules. Fundamentals of Protein NMR Spectroscopy is a comprehensive textbook that guides the reader from a basic understanding of the phenomenological properties of magnetic resonance to the application and interpretation of modern multi-dimensional NMR experiments on 15N/13C-labeled proteins. Beginning with elementary quantum mechanics, a set of practical rules is presented and used to describe many commonly employed multi-dimensional, multi-nuclear NMR pulse sequences. A modular analysis of NMR pulse sequence building blocks also provides a basis for understanding and developing novel pulse programs. This text not only covers topics from chemical shift assignment to protein structure refinement, as well as the analysis of protein dynamics and chemical kinetics, but also provides a practical guide to many aspects of modern spectrometer hardware, sample preparation, experimental set-up, and data processing. End of chapter exercises are included to emphasize important concepts. Fundamentals of Protein NMR Spectroscopy not only offer students a systematic, in-depth, understanding of modern NMR spectroscopy and its application to biomolecular systems, but will also be a useful reference for the experienced investigator.


List of Figures. List of Tables.
1. Introduction To NMR Spectroscopy.
2. Acquiring One-Dimensional Spectra.
3. Processing One-Dimensional Spectra.
4. Quantum Mechanical Description Of NMR.
5. Quantum Mechanical Description Of A One Pulse Experiment.
6. The Density Matrix.
7. Scalar Coupling.
8. Density Matrix And Product Operator of Coupled Spins.
9. Two Dimensional J-Correlations.
10. Heteronuclear J-Correlation Spectroscopy.
11. Coherence Editing.
12. Quadrature Detection In two Dimensional NMR Spectroscopy.
13. Exchange Processes.
14. Nuclear Spin Relaxation.
15. Resonance Assignments: Homonuclear Methods.
16. Resonance Assignments: Heteronuclear Methods.
17. Practical Aspects of N-Dimensional Data Acquisition And Processing.
18. Dipolar Coupling.
19. Protein Structure Determination.
A Fourier Transforms. B Complex Variables. C Solving Simultaneous Differential Equations: Laplace Transforms.


Professor of Biological Sciences at Carnegie Mellon University.
Professor Rule's research is directed at understanding inter-molecular interactions in biological systems. An understanding of these interactions is required if biological systems are to be comprehended at the molecular level. The combined tools of molecular biology, NMR spectroscopy and x-ray crystallography are used to provide important information to aid in our understanding of these interactions. Our research efforts have been directed at enzyme-substrate interactions, protein-lipid interactions, antibody-antigen interactions, and protein-nucleic acid interactions


From the reviews:
"I think this may become a very useful addition to the repertoire of books on biomolecular NMR spectroscopy. This text is more complete than the well-known book by Cavanagh et al., in the derivation of theoretical results and at the same time it contains more practical information. It is more up to date compared with the 1996 edition of Cavanagh (for instance by including residual dipolar couplings) and the inclusion of exercises is also an attractive feature."
(Prof. Dr. Rob Kaptein, Bijvoet Center for Biomolecular Research, The Netherlands)
EAN: 9781402034992
ISBN: 1402034997
Untertitel: Sprache: Englisch.
Verlag: Springer-Verlag GmbH
Erscheinungsdatum: Oktober 2005
Seitenanzahl: XXVI
Format: gebunden
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