Spin relaxation parameters, although difficult to interpret, are attracting interest in NMR as these parameters are capable of yielding both structural and dynamic information. Cross-relaxation and cross-correlation parameters afford a non-ambiguous approach to molecular structure and dynamics although they require some special skills for their experimental determination and for their exploitation. This work will start with an introduction to nuclear spin cross-relaxation and cross-correlation phenomena in liquids then look in more detail at molecules in soft matter and large biomolecules. Providing a detailed, timely account, the authors are filling a gap in the present NMR literature for the analytical scientist.

This work will provide a detailed account of cross-relaxation and cross-correlation which would be timely and fill a gap in the present NMR literature for the analytical scientist.

As a spectroscopic method, Nuclear Magnetic Resonance (NMR) has seen spectacular growth over the past two decades, both as a technique and in its applications. Today the applications of NMR span a wide range of scientific disciplines, from physics to biology to medicine. Each volume of Nuclear Magnetic Resonance comprises a combination of annual and biennial reports which together provide comprehensive of the literature on this topic. This Specialist Periodical Report reflects the growing volume of published work involving NMR techniques and applications, in particular NMR of natural macromolecules which is covered in two reports: "NMR of Proteins and Acids" and "NMR of Carbohydrates, Lipids and Membranes". For those wanting to become rapidly acquainted with specific areas of NMR, this title provides unrivalled scope of coverage. Seasoned practitioners of NMR will find this an in valuable source of current methods and applications. Specialist Periodical Reports provide systematic and detailed review coverage in major areas of chemical research. Compiled by teams of leading authorities in the relevant subject areas, the series creates a unique service for the active research chemist, with regular, in-depth accounts of progress in particular fields of chemistry. Subject coverage within different volumes of a given title is similar and publication is on an annual or biennial basis.

Nuclear magnetic resonance (NMR) is widely used across many fields of science because of the rich data it produces, and some of the most valuable data come from studies of nuclear spin relaxation in solution. The first edition of this book, published more than a decade ago, provided an accessible and cohesive treatment of the field. The present second edition is a significant update, covering important new developments in recent years. Collecting relaxation theory, experimental techniques, and illustrative applications into a single volume, this book clarifies the nature of the phenomenon, shows how to study it and explains why such studies are worthwhile. Coverage ranges from basic to rigorous theory and from simple to sophisticated experimental methods. Topics include cross-relaxation, multispin phenomena, relaxation studies of molecular dynamics and structure and special topics such as relaxation in systems with quadrupolar nuclei, in paramagnetic systems and in long-living spin states. Avoiding overly demanding mathematics, the authors explain spin relaxation in a manner that anyone with a familiarity with NMR can follow. The focus is on illustrating and explaining the physical nature of relaxation phenomena. Nuclear Spin Relaxation in Liquids: Theory, Experiments and Applications, 2nd edition, provides useful supplementary reading for graduate students and is a valuable reference for NMR spectroscopists, whether in chemistry, physics or biochemistry.

NMR has become the most diverse spectroscopic tool available to date in biomedical research. It is now routinely used to study biomolecular structure and dynamics particularly as a result of recent developments of a cascade of highly sophisticated multidimensional NMR pulse sequences, and of advances in genetic engineering to produce biomolecules, uniformly or selectively enriched with 13C, 15N and 2H.Features of this book:• Provides an up-to-date treatment of NMR techniques and their application to problems of biomedical interest• Most refined multidimensional pulse sequences including the basic aspects are covered by leading NMR spectroscopists.The book will be useful to NMR spectroscopists, biochemists, and to molecular biologists interested in the use of NMR techniques for solving biological problems.

The idea that a long-lived form of spin order, namely singlet order, can be prepared from nuclear spin magnetisation first emerged in 2004. The unusual properties of singlet order–its long lifetime and the fact that it is NMR silent but interconvertible into other forms of NMR active order—make it a ‘smart tag’ that can be used to store information for a long time or through distant space points. It is not unexpected then, that since its first appearance, this idea has caught the attention of research groups interested in exploiting this form of order in different fields of research spanning from biology to materials science and from hyperpolarisation to quantum computing. This first book on the subject gives a thorough description of the various aspects that affect the development of the topic and details the interdisciplinary applications. The book starts with a section dedicated to the basic theories of long-lived spin order and then proceeds with a description of the state-of-the-art experimental techniques developed to manipulate singlet order. It then concludes by covering the generalization of the concept of singlet order by introducing and discussing other forms of long-lived spin order.

Nuclear Magnetic Resonance Probes of Molecular Dynamics describes the theoretical basis and experimental techniques that make modern NMR spectroscopy a powerful and flexible tool for probing molecular dynamics in chemical, physical, and biochemical systems. Individual chapters, written by leaders in the development and application of NMR from around the world, treat systems that range from synthetic polymers, liquid crystals, and catalysts to proteins and oligonucleotides and techniques that include deuterium NMR, magic angle spinning, multidimensional spectroscopy, and magnetic resonance imaging. A combination of elementary and advanced material makes the book a useful introduction to the field for students at the graduate level as well as an important reference for practising NMR spectroscopists.

The vast progress made in the investigation of biomolecules using NMR has only recently been rewarded with the Nobel Prize for Kurt Wüthrich. Edited by a former coworker of Wüthrich, this book presents the theoretical background on NMR of biomolecules, plus the use of NMR techniques in determining the structures of proteins and nucleic acids. BioNMR spectroscopy offers a universal tool for examining the binding of an active substance to its target protein. Its use thereby benefits the rational development of drugs. This interaction can now be investigated in a hitherto unparalleled precision and displayed in 3D - an important prerequisite for the targeted development of new active substances. The latest methods for characterizing substance-receptor complexes are demonstrated backed by many case studies from pharmaceutical research. Thus it comes as no surprise that a large number of the authors are working for leading pharmaceutical companies. With its successful mixture of basic information and application strategies, coupled with many real-life examples, this is an invaluable guide for both NMR spectroscopists and pharmaceutical researchers.

Determination of structures of larger proteins in solution by three- and four-dimensional heteronuclear magnetic resonance spectroscopy. Methodological advances in protein NMR. Determination of high-resolution NMR structures of proteins. Multidimensional NMR studies of immunosuppressant/immunophilin complexes. NMR studies of the structure and role of modules involved in protein-protein interactions. NMR structural studies of membrane proteins. Heteronuclear NMR studies of the molecular synamics of staphylococcal nuclease. Study of protein dynamics by NMR. The folding, stability and dynamics of T4 lysozyme: a perspective using nuclear magnetic resonance.

The Encyclopedia of Biophysics is envisioned both as an easily accessible source of information and as an introductory guide to the scientific literature. It includes entries describing both Techniques and Systems. In the Techniques entries, each of the wide range of methods which fall under the heading of Biophysics are explained in detail, together with the value and the limitations of the information each provides. Techniques covered range from diffraction (X-ray, electron and neutron) through a wide range of spectroscopic methods (X-ray, optical, EPR, NMR) to imaging (from electron microscopy to live cell imaging and MRI), as well as computational and simulation approaches. In the Systems entries, biophysical approaches to specific biological systems or problems – from protein and nucleic acid structure to membranes, ion channels and receptors – are described. These sections, which place emphasis on the integration of the different techniques, therefore provide an inroad into Biophysics from a biological more than from a technique-oriented physical/chemical perspective. Thus the Encyclopedia is intended to provide a resource both for biophysicists interested in methods beyond those used in their immediate sub-discipline and for those readers who are approaching biophysics from either a physical or biological background.