Understanding NMR Spectroscopy: Edition 2

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This text is aimed at people who have some familiarity with high-resolution NMR and who wish to deepen their understanding of how NMR experiments actually ‘work’. This revised and updated edition takes the same approach as the highly-acclaimed first edition. The text concentrates on the description of commonly-used experiments and explains in detail the theory behind how such experiments work. The quantum mechanical tools needed to analyse pulse sequences are introduced set by step, but the approach is relatively informal with the emphasis on obtaining a good understanding of how the experiments actually work. The use of two-colour printing and a new larger format improves the readability of the text. In addition, a number of new topics have been introduced:
  • How product operators can be extended to describe experiments in AX2 and AX3 spin systems, thus making it possible to discuss the important APT, INEPT and DEPT experiments often used in carbon-13 NMR.
  • Spin system analysis i.e. how shifts and couplings can be extracted from strongly-coupled (second-order) spectra.
  • How the presence of chemically equivalent spins leads to spectral features which are somewhat unusual and possibly misleading, even at high magnetic fields.
  • A discussion of chemical exchange effects has been introduced in order to help with the explanation of transverse relaxation.
  • The double-quantum spectroscopy of a three-spin system is now considered in more detail.

Reviews of the First Edition

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

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

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About the author

Dr James Keeler is a Senior Lecturer in Chemistry at the University of Cambridge, and a Fellow of Selwyn College. In addition to being actively involved in the development of new NMR techniques, he is also responsible for the undergraduate chemistry course, and is Editor-In-chief of Magnetic Resonance in Chemistry. Dr Keeler is well-known for his clear and accessible exposition of NMR spectroscopy.
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Additional Information

Publisher
John Wiley & Sons
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Published on
Sep 19, 2011
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Pages
526
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ISBN
9781119964933
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Language
English
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Genres
Science / Chemistry / General
Science / Spectroscopy & Spectrum Analysis
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Content Protection
This content is DRM protected.
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Malcolm H. Levitt
Spin Dynamics: Basics of Nuclear Magnetic Resonance, Second Edition is a comprehensive and modern introduction which focuses on those essential principles and concepts needed for a thorough understanding of the subject, rather than the practical aspects. The quantum theory of nuclear magnets is presented within a strong physical framework, supported by figures. 

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

Completely revised and updated, the Second Edition features new material on the properties and distributions of isotopes, chemical shift anisotropy and quadrupolar interactions, Pake patterns, spin echoes, slice selection in NMR imaging, and a complete new chapter on the NMR spectroscopy of quadrupolar nuclei. New appendices have been included on Euler angles, and coherence selection by field gradients. As in the first edition, all material is heavily supported by graphics, much of which is new to this edition. 

Written for undergraduates and postgraduate students taking a first course in NMR spectroscopy and for those needing an up-to-date account of the subject, this multi-disciplinary book will appeal to chemical, physical, material, life, medical, earth and environmental scientists. The detailed physical insights will also make the book of interest for experienced spectroscopists and NMR researchers. 

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

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

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

• Includes numerous worked examples, problems, further reading and additional notes

Praise from the reviews of the First Edition:

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

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

L. D. Field
The derivation of structural information from spectroscopic data is now an integral part of organic chemistry courses at all Universities.  A critical part of any such course is a suitable set of problems to develop the student’s understanding of how structures are determined from spectra. 

Organic Structures from Spectra, Fifth Edition is a carefully chosen set of more than 280 structural problems employing the major modern spectroscopic techniques, a selection of 27 problems using 2D-NMR spectroscopy, more than 20 problems specifically dealing with the interpretation of spin-spin coupling in proton NMR spectra and 8 problems based on the quantitative analysis of mixtures using proton and carbon NMR spectroscopy.  All of the problems are graded to develop and consolidate the student’s understanding of organic spectroscopy.  The accompanying text is descriptive and only explains the underlying theory at a level which is sufficient to tackle the problems.  The text includes condensed tables of characteristic spectral properties covering the frequently encountered functional groups.

The examples themselves have been selected to include all important common structural features found in organic compounds and to emphasise connectivity arguments.  Many of the compounds were synthesised specifically for this purpose.  There are many more easy problems, to build confidence and demonstrate basic principles, than in other collections. 

The fifth edition of this popular textbook:

• includes more than 250 new spectra and more than 25 completely new problems;
• now incorporates an expanded suite of new problems dealing with the analysis of 2D NMR spectra (COSY, C H Correlation spectroscopy, HMBC, NOESY and TOCSY); 
• has been expanded and updated to reflect the new developments in NMR and to retire older techniques that are no longer in common use;
• provides a set of problems dealing specifically with the quantitative analysis of mixtures using NMR spectroscopy;
• features proton NMR spectra obtained at 200, 400 and 600 MHz and 13C NMR spectra include DEPT experiments as well as proton-coupled experiments;
• contains 6 problems in the style of the experimental section of a research paper and two examples of fully worked solutions.

Organic Structures from Spectra, Fifth Edition will prove invaluable for students of Chemistry, Pharmacy and Biochemistry taking a first course in Organic Chemistry.

Contents
Preface 
Introduction 
Ultraviolet Spectroscopy 
Infrared Spectroscopy
Mass Spectrometry 
Nuclear Magnetic Resonance Spectroscopy 
2DNMR
Problems 
Index

Reviews from earlier editions

“Your book is becoming one of the “go to” books for teaching structure determination here in the States.  Great work!”

“…I would definitely state that this book is the most useful aid to basic organic spectroscopy teaching in existence and I would strongly recommend every instructor in this area to use it either as a source of examples or as a class textbook”.
Magnetic Resonance in Chemistry

“Over the past year I have trained many students using problems in your book - they initially find it as a task.  But after doing 3-4 problems with all their brains activities... working out the rest of the problems become a mania.  They get addicted to the problem solving and every time they solve a problem by themselves, their confident level also increases.”

 “I am teaching the fundamentals of Molecular Spectroscopy and your books represent excellent sources of spectroscopic problems for students.”

John Cavanagh
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 spectroscopyDemonstrates how to implement, optimize and troubleshoot modern multi-dimensional NMR experimentsAllows for the capability of designing effective experimental protocols for investigations of protein structures and dynamicsIncludes a comprehensive set of example NMR spectra of ubiquitin provides a reference for validation of experimental methods
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