This book presents a critical assessment of progress on the use of nuclear magnetic resonance spectroscopy to determine the structure of proteins, including brief reviews of the history of the field along with coverage of current clinical and in vivo applications. The book, in honor of Oleg Jardetsky, one of the pioneers of the field, is edited by two of the most highly respected investigators using NMR, and features contributions by most of the leading workers in the field. It will be valued as a landmark publication that presents the state-of-the-art perspectives regarding one of today's most important technologies.
‘‘Biopolymers’’ are polymeric materials of biological origin, including globular, membrane, and fibrous proteins, polypeptides, nucleic acids, po- saccharides, lipids, etc. and their assembly, although preference to respe- ive subjects may be different among readers who are more interested in their biological significance or industrial and/or medical applications. Nevert- less, characterizing or revealing their secondary structure and dynamics may be an equally very important and useful issue for both kinds of readers. Special interest in revealing the 3D structure of globular proteins, nucleic acids, and peptides was aroused in relation to the currently active Structural Biology. X-ray crystallography and multidimensional solution NMR sp- troscopy have proved to be the standard and indispensable means for this purpose. There remain, however, several limitations to this end, if one intends to expand its scope further. This is because these approaches are not always straightforward to characterize fibrous or membrane proteins owing to extreme difficulty in crystallization in the former, and insufficient spectral resolution due to sparing solubility or increased effective molecular mass in the presence of surrounding lipid bilayers in the latter.
Advances in Biological NMR brings the reader up to date with chapters from international leaders of this growing field, covering the most recent developments in the methodology and applications of solid state NMR to studies of membrane interactions and molecular motions
Over the past decade, a myriad of techniques have shown that solid-state nuclear magnetic resonance (NMR) can be used in a broad spectrum of applications with exceptionally impressive results. Solid-state NMR results can yield high-resolution details on the structure and function of many important biological solids, including viruses, fibril-formin
The purpose of this book is to describe the methodology and applications of solid-state NMR spectroscopy to studies of membrane proteins, membrane-active peptides and model biological membranes. As well as structural studies, this book contains coverage of membrane interactions and molecular motions. Advances in biological solid-state NMR are very pertinent with high-field developments seeing applications in biological membranes and whole cells. Experts who are leaders in the development and application of biological solid-state NMR are chapter contributors. Part of Biophysical Society-IOP series.
NMR spectroscopy is the most valuable and versatile analytical tool in chemistry. While excellent monographs exist on high-resolution NMR in liquids and solids, this is the first book to address multidimensional solid-state NMR. Multidimensional techniques enable researchers to obtain detailed information about the structure, dynamics, orientation, and phase separation of solids, which provides the basis of a better understanding of materials properties on the molecular level.Dramatic progress-much of it pioneered by the authors-has been achieved in this area, especially in synthetic polymers. Solid-state NMR now favorably competes with well-established techniques, such as light, x-ray, or neutron scattering, electron microscopy, and dielectric and mechanical relaxation.The application of multidimensional solid-state NMR inevitably involves use of concepts from different fields of science. This book also provides the first comprehensive treatment of both the new experimental techniques and the theoretical concepts needed in more complex data analysis. The text addresses spectroscopists and polymer scientists by treating the subject on different levels; descriptive, technical, and mathematical approaches are used when appropriate. It presents an overview of new developments with numerous experimental examples and illustrations, which will appeal to readers interested in both the information content as well as the potential of solid-state NMR. The book also contains many previously unpublished details that will be appreciated by those who want to perform the experiments. The techniques described are applicable not only to the study of synthetic polymers but to numerous problems in solid-state physics, chemistry, materials science, and biophysics. - Presents original theories and new perspectives on scattering techniques - Provides a systematic treatment of the whole subject - Gives readers access to previously unpublished material - Includes extensive illustrations
This volume is an ideal starting point for the graduate student seeking a basic introduction to the theory and uses of solid-state nuclear magnetic resonance (NMR) spectroscopy. Accessible to students with only a survey-level physics background, the material assumes little prior knowledge of the basic theory of electromagnetism. All the major areas are covered, including an introduction to concepts of time-dependent quantum mechanics as they apply to NMR spectroscopy of the solid state. Each chapter includes problems designed to enhance the reader's understanding of the material. Instructive and practical, this volume provides the basic knowledge needed to access the general literature and the more advanced monographs on this subject. In addition to assisting entrance into the field, Transient Techniques in NMR of Solids will be a useful guide for professionals already working in related areas of chemistry. FROM THE PREFACE: Nuclear magnetic resonance (NMR) is truly a remarkable phenomenon. Remarkable can imply different things to different people. From the point of view of a physicist, spin dynamics is an elegant example of the use of time-dependent quantum mechanics, and NMR absorption of energy is a prototype for spectroscopic transitions. From the point of view of the practicing chemist and materials scientist, NMR spectroscopy is an invaluable tool for the identification of chemical species and structures. Had NMR spectroscopic techniques commercially available in the early 1960s been the only result of investigations of this phenomenon, it would have had a major impact on the course of chemical analysis. The study of liquids and solutions for chemical shifts and couplings of protons had produced a rapid means of identifying chemical species nondestructively. The study of dynamical properties also could be addressed by study of temperature dependence of the spectra or of the saturation of the resonance by high-power irradiation. Even at that time, however, studies of the spin dynamics had already begun to indicate that there were many interesting facets of the NMR phenomenon left to exploit. For example, the Fourier-transform relationship of the free-induction decay and the absorption spectrum had been shown and the basis of the cross-polarization experiment was being investigated. A number of chemists had begun to study the spin*b1lattice relaxation times of species by pulse NMR techniques by utilizing methods that were not familiar at that time to the typical chemist but that are now commonly employed in NMR analysis. The principal characteristic of the NMR technique that makes it so useful for chemical analysis of liquids and solutions is the high resolution that allows one to observe very small interactions such as the chemical shift and the spin*b1spin coupling. These weak interactions are quite sensitive to the local environment of the spin and therefore may be used as a diagnostic for the environment. The connectivity of chemical structure is often mimicked closely in the NMR connectivity of the spectrum, and quantitative informaton is relatively easy to obtain. Nuclear magnetic resonance spectra of solids exhibit such resolution only in special cases. The primary (although not the exclusive) reason for the lack of resolution in the spectrum of a typical solid is the presence of the dipole*b1dipole interaction, which dominates the NMR spectroscopy of solids that have been of interest to chemists. One solution (no pun intended) to the problem of obtaining chemical-shift information about such solids is to dissolve them and to study them in solution. However, if the solid is insoluble or otherwise intractable or if the analysis involves questions about the properties of the substance in the solid state, then there arises a need for techniques to study the weaker interactions in the presence of the dipole*b1dipole interaction or other overwhelming interactions. This volume describes the means dev
This book is for those familiar with solution-state NMR who are encountering solid-state NMR for the first time. It presents the current understanding and applications of solid-state NMR with a rigorous but readable approach, making it easy for someone who merely wishes to gain an overall impression of the subject without details. This dual requirement is met through careful construction of the material within each chapter. The book is divided into two parts: "Fundamentals" and "Further Applications." The section on Fundamentals contains relatively long chapters that deal with the basic theory and practice of solid-state NMR. The essential differences and extra scope of solid-state NMR over solution-state is dealt with in an introductory chapter. The basic techniques that all chapters rely on are collected into a second chapter to avoid unnecessary repetition later. Remaining chapters in the "Fundamentals" part deal with the major areas of solid-state NMR which all solid-state NMR spectroscopists should know about. Each begins with an overview of the topic that puts the chapter in context. The basic principles upon which the techniques in the chapter rely are explained in a separate section. Each of these chapters exemplifies the principles and techniques with the applications most commonly found in current practice. The "Further Applications" section contains a series of shorter chapters which describe the NMR techniques used in other, more specific areas. The basic principles upon which these techniques rely will be expounded only if not already in the Fundamentals part.
In polymer science and technology, the advanced development of various new polymer materials with excellent properties and functions is desirable. For this purpose it is necesary to determine the exact relationship between physical properties and molecular structure-dynamics with powerful techniques. One such technique is solid state NMR. Recently, high resolution NMR studies of solids have been realized by using advanced pulse and mechanical techniques, which has resulted in a variety of structural and dynamical information on polymer systems. Solid state NMR has provided characteristic information which cannot be obtained by other spectroscopic methods.This book is divided into two parts. The first part covers the principles of NMR, important NMR parameters such as chemical shifts, relaxation times, dipolar interactions, quadrupolar interactions, pulse techniques and new NMR methods. In the second part, applications of NMR to a variety of polymer systems in the solid state are described.Features of this book:• Contains an up-to-date and comprehensive account of solid state NMR of polymers by leading researchers in the field• Provides a compilation of solid state NMR of polymers, which makes it an ideal reference book for both NMR researchers and general polymer scientists.This book will be of interest to the NMR community, and will be invaluable for both the beginner and the expert.
The technique of nuclear magnetic resonance (NMR) spectroscopy is an important tool in biochemistry and biophysics for the understanding of the structure and ultimately, the function of biomolecules. This textbook explains the salient features of biological NMR spectroscopy to undergraduates and postgraduates taking courses in NMR, biological NMR, physical biochemistry, and biophysics. Unlike other books in the general field of NMR (except the advanced treatises), the approach here is tointroduce and make use of quantum mechanical product operators as well as the classical vector method of explaining the bewildering array of pulse sequences available today. The book covers two- dimensional, three- dimensional, and four- dimensional NMR and their application to protein and DNA structure determination. A unique feature is the coverage of the biological aspects of solid- state NMR spectroscopy. The author provides many selected examples from the research literature, illustratingthe applications of NMR spectroscopy to biological proteins.
