Protein NMR Spectroscopy: Principles and Practice, Edition 2

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Protein NMR Spectroscopy, Second Edition 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, the book 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. This updated version 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.

The book is written as a graduate-level textbook and will be of interest to biochemists, chemists, biophysicists, and structural biologists who utilize NMR spectroscopy or 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
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About the author

Dr. Cavanagh is the William Neal Reynolds Distinguished Professor of Biochemistry at North Carolina State University. He is an expert in protein structural biology, particularly in how bacteria are able to protect themselves. Dr. Cavanagh received his Ph.D. in Chemistry/NMR spectroscopy from the University of Cambridge in 1988. He has held positions as a Senior Research Associate at The Scripps Research Institute, Director of Structural Biology at the Wadsworth Center (New York State Department of Health), Associate Professor of Biomedical Sciences (SUNY) and Professor of Chemistry (Purdue). Since 2000 he has been Professor of Biochemistry in the Department of Molecular & Structural Biochemistry at North Carolina State University. Dr. Cavanagh has served on numerous NIH and NSF grant review panels and is currently a permanent member of the MSFB Study Section at NIH . He has authored over 100 peer-reviewed research publications and has been awarded the Foulerton Gift & Binmore Kenner Fellowship of the Royal Society (1990), the Fullsome Award (1996), the NC State University Alumni Associations Outstanding Research Award (2005) and Entrepreneur of the Year- NC State University (2012). He runs the Jimmy V-NCSU Cancer Therapeutics Training Program, was Assistant Vice Chancellor for Research at NC State from 2012-2014 and is the co-founder and Chief Scientific Officer of Agile Sciences Inc., a Raleigh based biotechnology company focusing on antibiotic resistance.

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Additional Information

Publisher
Elsevier
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Published on
Jul 21, 2010
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Pages
912
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ISBN
9780080471037
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Language
English
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Genres
Science / Chemistry / Analytic
Science / Life Sciences / Biochemistry
Science / Life Sciences / Cell Biology
Science / Spectroscopy & Spectrum Analysis
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Content Protection
This content is DRM protected.
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Available on Android devices
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Eligible for Family Library

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This text is aimed at people who have some familiarity withhigh-resolution NMR and who wish to deepen their understanding ofhow NMR experiments actually ‘work’. This revised andupdated edition takes the same approach as the highly-acclaimedfirst edition. The text concentrates on the description ofcommonly-used experiments and explains in detail the theory behindhow such experiments work. The quantum mechanical tools needed toanalyse pulse sequences are introduced set by step, but theapproach is relatively informal with the emphasis on obtaining agood understanding of how the experiments actually work. The use oftwo-colour printing and a new larger format improves thereadability of the text. In addition, a number of new topics havebeen introduced: How product operators can be extended to describe experimentsin AX2 and AX3 spin systems, thus making it possible to discuss theimportant APT, INEPT and DEPT experiments often used in carbon-13NMR.Spin system analysis i.e. how shifts and couplings can beextracted from strongly-coupled (second-order) spectra.How the presence of chemically equivalent spins leads tospectral features which are somewhat unusual and possiblymisleading, even at high magnetic fields.A discussion of chemical exchange effects has been introducedin order to help with the explanation of transverserelaxation.The double-quantum spectroscopy of a three-spin system is nowconsidered in more detail.

Reviews of the First Edition

“For anyone wishing to know what really goes on in theirNMR experiments, I would highly recommend this book” –Chemistry World

“…I warmly recommend for budding NMRspectroscopists, or others who wish to deepen their understandingof elementary NMR theory or theoretical tools” –Magnetic Resonance in Chemistry

Spin Dynamics: Basics of Nuclear Magnetic Resonance, SecondEdition is a comprehensive and modern introduction whichfocuses on those essential principles and concepts needed for athorough understanding of the subject, rather than the practicalaspects. The quantum theory of nuclear magnets is presented withina strong physical framework, supported by figures. 

The book assumes only a basic knowledge of complex numbers andmatrices, and provides the reader with numerous worked examples andexercises to encourage understanding. With the explicit aim ofcarefully developing the subject from the beginning, the textstarts with coverage of quarks and nucleons and progresses throughto a detailed explanation of several important NMR experiments,including NMR imaging, COSY, NOESY and TROSY. 

Completely revised and updated, the Second Edition features newmaterial on the properties and distributions of isotopes, chemicalshift anisotropy and quadrupolar interactions, Pake patterns, spinechoes, slice selection in NMR imaging, and a complete new chapteron the NMR spectroscopy of quadrupolar nuclei. New appendices havebeen included on Euler angles, and coherence selection by fieldgradients. As in the first edition, all material is heavilysupported by graphics, much of which is new to thisedition. 

Written for undergraduates and postgraduate students taking afirst course in NMR spectroscopy and for those needing anup-to-date account of the subject, this multi-disciplinary bookwill appeal to chemical, physical, material, life, medical, earthand environmental scientists. The detailed physical insights willalso make the book of interest for experienced spectroscopists andNMR researchers. 

• An accessible and carefully written introduction,designed to help students to fully understand this complex anddynamic subject

• Takes a multi-disciplinary approach, focusing on basicprinciples and concepts rather than the more practical aspects

• Presents a strong pedagogical approach throughout, withemphasis placed on individual spins to aid understanding

• Includes numerous worked examples, problems, furtherreading and additional notes

Praise from the reviews of the First Edition:

"This is an excellent book... that many teachers of NMRspectroscopy will cherish... It deserves to be a‘classic’ among NMR spectroscopy texts." NMRIN BIOMEDICINE

"I strongly recommend this book to everyone…it isprobably the best modern comprehensive description of thesubject." ANGEWANDTE CHEMIE, INTERNATIONAL EDITION

Protein NMR Spectroscopy: Principles and Practice combines a comprehensive theoretical treatment of high resolution NMR spectroscopy with an extensive exposition of the experimental techniques applicable to proteins and other biological macromolecules. Beginning with simple theoretical models and experimental techniques, Protein NMR Spectroscopy: Principles and Practice develops the complete repertoire of theoretical principals and experimental practices necessary for understanding and implementing the most sophisticated NMR experiments. Protein NMR Spectroscopy: Principles and Practice is written as a graduate-level textbook and will be of particular interest to biochemists, chemists, biophysicists, and structural biologists who utilize NMR spectroscopy as a research tool or who wish to remain abreast of the latest developments in this increasingly important area.

* Special Features:
* First book to combine detailed NMR theory discussions with experimental applications to biomolecules.
* All the theory required to understand these experiments and others.
* Easy to follow progression from a fundamental level to an advanced level.
* Theory of NMR and practical applications for biomolecular investigations presented.
* Theory applied to very practical situations.
* Comprehensive treatment of different "levels" of theory from simple ideas to density matrix analysis and operator practices.
* Comprehensive description of multi dimensional NMR experiments as applied to unlabeled, 15N-labeled and doubly (13C/15N) labeled proteins.
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