Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful and theoretically complex analytical tool. Basic 1H- and 13C-NMR Spectroscopy provides an introduction to the principles and applications of NMR spectroscopy. Whilst looking at the problems students encounter when using NMR spectroscopy, the author avoids the complicated mathematics that are applied within the field. Providing a rational description of the NMR phenomenon, this book is easy to read and is suitable for the undergraduate and graduate student in chemistry. - Describes the fundamental principles of the pulse NMR experiment and 2D NMR spectra - Easy to read and written with the undergraduate and graduate chemistry student in mind - Provides a rational description of NMR spectroscopy without complicated mathematics

FROM THE PREFACE: Pulse Methods in 1D and 2D Liquid-Phase NMR is written to enable the practicing NMR spectroscopist to understand and apply the varied and powerful new techniques developed in the past few years for obtaining spectra with greatly increased information content and from smaller and smaller samples. The intent is to describe both theory and practice in simple and detailed fashion so that the methods may be critically evaluated and effectively used in any potential application. As methods become more complex they require more instrument time, and it is important to be able to judge whether the investment of this time is justified. It is also essential for the spectroscopist to be in a position to evaluate the capabilities of the instrumentation available, as well as the additional requirements for utilization of particular new methods. The material in this book assumes a knowledge of continuous-wave NMR methods as well as an elementary understanding of the normal pulsed Fourier-transform spectroscopic procedures, together with a knowledge of such related phenomena as the nuclear Overhauser effect. Although much of the treatment is necessarily methematical, this aspect of the presentation has been simplified as much as possible.

This work-book will guide you safely, in step-by-step descriptions, through every detail of the NMR experiments within, beginning with 1D routine experiments and ending with a series of advanced 3D experiments on a protein: ? Which experiment can best yield the desired information? ? How must the chosen experiment be performed? ? How does one read the required information from the spectrum? ? How does this particular pulse sequence work? ? Which other experiments give similar information? This third edition of the book, following its two highly successful predecessors, has been revised and expanded to 206 experiments. They are organized in 15 chapters, covering test procedures and routine spectra, variable temperature measurements, the use of auxiliary reagents, 1D multipulse experiments, spectra of heteronuclides, and the application of selective pulses. The second and third dimensions are introduced using pulsed field gradients, and experiments on solid state materials are described. A key part describes 3D experiments on the protein ubiquitin with 76 amino acids. What is new in this third edition? 1. 24 new experiments have been inserted into the 14 chapters that were in the 2nd edition, e.g., alpha/beta-SELINCOR-TOCSY, WET, DOSY, ct-COSY, HMSC, HSQC with adiabatic pulses, HETLOC. J-resolved HMBC, (1,1)- and (1,n)-ADEQUATE, STD, REDOR, and HR-MAS. 2. 20 new protein NMR experiments have been specially devised and are collected in the newly added Chapter 15, ProteinNMR, for which one needs a special model sample: fully 13C- and 15N-labeled human ubiquitin. Techniques used include the constant time principle, the PEP method, filters, gradient selection, and the echo/anti-echo procedure. The guide has been written by experts in this field, following the principle of learning by doing: all the experiments have been specially performed for this book, exactly as described and shown in the spectra that are reproduced. Being a reference source and work-book for the NMR laboratory as well as a textbook, it is a must for every scientist working with NMR, as well as for students preparing for their laboratory courses

From the initial observation of proton magnetic resonance in water and in paraffin, the discipline of nuclear magnetic resonance has seen unparalleled growth as an analytical method. Modern NMR spectroscopy is a highly developed, yet still evolving, subject which finds application in chemistry, biology, medicine, materials science and geology. In this book, emphasis is on the more recently developed methods of solution-state NMR applicable to chemical research, which are chosen for their wide applicability and robustness. These have, in many cases, already become established techniques in NMR laboratories, in both academic and industrial establishments. A considerable amount of information and guidance is given on the implementation and execution of the techniques described in this book.

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.

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