Fundamentals of Protein NMR Spectroscopy

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 15 N/ 13 C-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 contents

NMR Spectroscopy.- Practical Aspects of Acquiring NMR Spectra.- to Signal Processing.- Quantum Mechanical Description of NMR.- Quantum Mechanical Description of a One Pulse Experiment.- The Density Matrix & Product Operators.- Scalar Coupling.- Coupled Spins: Density Matrix and Product Operator Formalism.- Two Dimensional Homonuclear J-Correlated Spectroscopy.- Two Dimensional Heteronuclear J-Correlated Spectroscopy.- Coherence Editing: Pulsed-Field Gradients and Phase Cycling.- Quadrature Detection in Multi-Dimensional NMR Spectroscopy.- Resonance Assignments: Homonuclear Methods.- Resonance Assignments: Heteronuclear Methods.- Practical Aspects of N-Dimensional Data Acquisition and Processing.- Dipolar Coupling.- Protein Structure Determination.- Exchange Processes.- Nuclear Spin Relaxation and Molecular Dynamics.

About the author

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

Summary

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.

Additional text

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)

Report

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)

Product details

• Authors: T Kevin Hitchens, T. K. Hitchens, T. Kevin Hitchens, T.Kevin Hitchens, G. S. Rule, Gordon Rule, Gordon S Rule, Gordon S. Rule
• Publisher: Springer Netherlands
• Languages: English
• Product format: Hardback
• Released: 30.12.2005
• EAN: 9781402034992
• ISBN: 978-1-4020-3499-2
• No. of pages: 532
• Dimensions: 166 mm x 239 mm x 38 mm
• Weight: 995 g
• Illustrations: XXVI, 532 p.
• Series: Focus on Structural Biology; Focus on Structural Biology
• Subject: Natural sciences, medicine, IT, technology > Biology > Biochemistry, biophysics