Ebook: 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 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.

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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.

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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.

Content:
Front Matter....Pages i-xxvi
NMR Spectroscopy....Pages 1-27
Practical Aspects of Acquiring NMR Spectra....Pages 29-64
Introduction to Signal Processing....Pages 65-88
Quantum Mechanical Description of NMR....Pages 89-112
Quantum Mechanical Description of a One Pulse Experiment....Pages 113-120
The Density Matrix & Product Operators....Pages 121-134
Scalar Coupling....Pages 135-151
Coupled Spins: Density Matrix and Product Operator Formalism....Pages 153-167
Two Dimensional Homonuclear J-Correlated Spectroscopy....Pages 169-195
Two Dimensional Heteronuclear J-Correlated Spectroscopy....Pages 197-211
Coherence Editing: Pulsed-Field Gradients and Phase Cycling....Pages 213-237
Quadrature Detection in Multi-Dimensional NMR Spectroscopy....Pages 239-250
Resonance Assignments: Homonuclear Methods....Pages 251-275
Resonance Assignments: Heteronuclear Methods....Pages 277-312
Practical Aspects of N-Dimensional Data Acquisition and Processing....Pages 313-351
Dipolar Coupling....Pages 353-381
Protein Structure Determination....Pages 383-402
Exchange Processes....Pages 403-430
Nuclear Spin Relaxation and Molecular Dynamics....Pages 431-474
Back Matter....Pages 475-531

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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.

Content:
Front Matter....Pages i-xxvi
NMR Spectroscopy....Pages 1-27
Practical Aspects of Acquiring NMR Spectra....Pages 29-64
Introduction to Signal Processing....Pages 65-88
Quantum Mechanical Description of NMR....Pages 89-112
Quantum Mechanical Description of a One Pulse Experiment....Pages 113-120
The Density Matrix & Product Operators....Pages 121-134
Scalar Coupling....Pages 135-151
Coupled Spins: Density Matrix and Product Operator Formalism....Pages 153-167
Two Dimensional Homonuclear J-Correlated Spectroscopy....Pages 169-195
Two Dimensional Heteronuclear J-Correlated Spectroscopy....Pages 197-211
Coherence Editing: Pulsed-Field Gradients and Phase Cycling....Pages 213-237
Quadrature Detection in Multi-Dimensional NMR Spectroscopy....Pages 239-250
Resonance Assignments: Homonuclear Methods....Pages 251-275
Resonance Assignments: Heteronuclear Methods....Pages 277-312
Practical Aspects of N-Dimensional Data Acquisition and Processing....Pages 313-351
Dipolar Coupling....Pages 353-381
Protein Structure Determination....Pages 383-402
Exchange Processes....Pages 403-430
Nuclear Spin Relaxation and Molecular Dynamics....Pages 431-474
Back Matter....Pages 475-531
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