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Used primarily for characterizing polymers and biological systems, vibrational spectroscopy continues to uncover structural information pertinent to a growing number of applications. Vibrational Spectroscopy of Biological and Polymeric Materials compiles the latest developments in advanced infrared and Raman spectroscopic techniques that are
An introduction to the physical principles of spectroscopy and their applications to the biological sciences Advances in such fields as proteomics and genomics place new demands on students and professionals to be able to apply quantitative concepts to the biological phenomena that they are studying. Spectroscopy for the Biological Sciences provides students and professionals with a working knowledge of the physical chemical aspects of spectroscopy, along with their applications to important biological problems. Designed as a companion to Professor Hammes's Thermodynamics and Kinetics for the Biological Sciences, this approachable yet thorough text covers the basic principles of spectroscopy, including: * Fundamentals of spectroscopy * Electronic spectra * Circular dichroism and optical rotary dispersion * Vibration in macromolecules (IR, Raman, etc.) * Magnetic resonance * X-ray crystallography * Mass spectrometry With a minimum of mathematics and a strong focus on applications to biology, this book will prepare current and future professionals to better understand the quantitative interpretation of biological phenomena and to utilize these tools in their work.
Spectroscopy in Biology and Chemistry discusses the use of thermal neutron diffraction and inelastic scattering, and the related techniques of x-ray diffraction, Raman and Rayleigh scattering, in investigating biological macromolecules and chemical systems. The book describes neutron, x-ray and laser spectroscopy; quasielastic scattering in neutron and laser spectroscopy; and interatomic forces, molecular structure and molecular vibrations. The text also discusses the x-ray crystallography of biological molecules; neutron diffraction studies of hydrogen bonding in organic and biochemical syste ...
During teaching NMR to students and researchers, we felt the need for a text-book which can cover modern trends in the application of NMR to biological systems. This book covers the entire area of NMR in Biological Sciences (Biomolecules, cells and tissues, animals, plants and drug design). As well as being useful to researchers, this is an excellent book for teaching a course on NMR in Biological Systems.
The authors describe basic theoretical concepts of vibrational spectroscopy, address instrumental aspects and experimental procedures, and discuss experimental and theoretical methods for interpreting vibrational spectra. It is shown how vibrational spectroscopy provides information on general aspects of proteins, such as structure, dynamics, and protein folding. In addition, the authors use selected examples to demonstrate the application of Raman and IR spectroscopy to specific biological systems, such as metalloproteins, and photoreceptors. Throughout, references to extensive mathematical and physical aspects, involved biochemical features, and aspects of molecular biology are set in boxes for easier reading. Ideal for undergraduate as well as graduate students of biology, biochemistry, chemistry, and physics looking for a compact introduction to this field.
In-cell NMR spectroscopy is a relatively new field. Despite its short history, recent in-cell NMR-related publications in major journals indicate that this method is receiving significant general attention. This book provides the first informative work specifically focused on in-cell NMR. It details the historical background of in-cell NMR, host cells for in-cell NMR studies, methods for in-cell biological techniques and NMR spectroscopy, applications, and future perspectives. Researchers in biochemistry, biophysics, molecular biology, cell biology, structural biology as well as NMR analysts interested in biological applications will all find this book valuable reading.
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.
Comprises ten carefully edited reviews of several aspects of biological systems, written by acknowledged leaders in their fields. Coverage is state-of-the-art and will satisfy the specialist's need to keep abreast of new developments. Material is presented in a manner which is comprehensible to the non-expert. A valuable introduction and a timely overview of topics in spectroscopy of current interest and importance.
Over the past several decades, vanadium has increasingly attracted the interest of biologists and chemists. The discovery by Henze in 1911 that certain marine ascidians accumulate the metal in their blood cells in unusually large quantities has done much to stimulate research on the role of vanadium in biology. In the intervening years, a large number of studies have been carried out to investigate the toxicity of vanadium in higher animals and to determine whether it is an essential trace element. That vanadium is a required element for a few selected organisms is now well established. Whether vanadium is essential for humans remains unclear although evidence increasingly suggests that it probably is. The discovery by Cantley in 1977 that vanadate is a potent inhibitor of ATPases lead to numerous studies of the inhibitory and stimulatory effects of vanadium on phosphate metabolizing enzymes. As a consequence vanadates are now routinely used as probes to investigate the mechanisms of such enzymes. Our understanding of vanadium in these systems has been further enhanced by the work of Tracy and Gresser which has shown striking parallels between the chemistry of vanadates and phosphates and their biological compounds. The observation by Shechter and Karlish, and Dubyak and Kleinzeller in 1980 that vanadate is an insulin mimetic agent has opened a new area of research dealing with the hormonal effects of vanadium. The first vanadium containing enzyme, a bromoperoxidase from the marine alga Ascophyllum nodosum, was isolated in 1984 by Viltner.
At the time that the editors conceived the idea of trying to organize the meeting on which the contents of this volume are based and which became, in March 1980, a NATO Advanced Study Institute, the techniques of time-resolved fluorescence spectroscopy, in both the nanosecond and sub-nanosecond time-domains, might reasonably have been said to be coming of age, both in their execution and in the analysis and interpretation of the results obtained. These techniques, then as now, comprised mainly a number of pulse methods using laser, flash-lamp or, most recently, synchrotron radiation. In addition, significant developments in the more classical phase approach had also rendered that method popular, utilizing either modulation of an otherwise continuous source or, again recently, the ultra-rapid pulse rate attainable with a synchrotron source. In general terms, time-resolved fluorescence studies are capable, under appropriate conditions, of supplying direct kinetic information on both photophysics and various aspects of molecular, macromolecular and supramolecular structure and dynamics. The nanosecond and sub-nanosecond time-scales directly probed render these techniques particularly appropriate in studying relaxation and fluctuation processes in macromolecules, particularly biopolymers (e. g. proteins, nucleic acids), in supramolecular assemblies such as cell membranes, and in a variety of relatively simpler model systems.