Epr Instrumental Methods

Electron magnetic resonance spectroscopy is undergoing something akin to a renaissance that is attributable to advances in microwave circuitry and signal processing software. EPR: Instrumental Methods is a textbook that brings the reader up to date on these advances and their role in providing better experimental techniques for biological magnetic resonance. Chapters in this book guide the reader from basic principles of spectrometer design through the advanced methods that are providing new vistas in disciplines such as oximetry, imaging, and structural biology. Key Features: Spectrometer design, particularly at low frequencies (below X-band), Design of spectrometer components unique to ENDOR and ESEEM, Optimization of EMR spectrometer sensitivity spanning many octaves, Algorithmic approach to spectral parameterization, Application of Fourier Methods to polymer conformation, oximetry, and imaging.

Computational and Instrumental Methods in EPR is devoted to both instrumentation and computation aspects of EPR, while addressing applications such as spin relaxation time measurements. However, this is the first comprehensive volume to offer practical, non-invasive spectroscopic methods of analyzing the rheology of biopolymers: comparative studies of polymer fluidity using traditional methods (e.g. viscosity) and nuclear magnetic resonance.

EPR spectroscopy is a versatile, nondestructive technique widely used in chemistry, biology, and physics. It detects molecules and materials with unpaired electrons making it a very selective technique that produces a wealth of information on such systems. Its high sensitivity makes it suitable in analyzing very small samples, single crystals, or reaction intermediates like radicals. This textbook takes a practical approach that introduces the basic concepts of EPR to sufficient detail to allow the reader to gain a basic knowledge of EPR and understand how experiments are carried out and how spectra are analyzed and interpreted. Many illustrative examples are included drawn from solid-state physics and bioinorganic chemistry. It is suitable as a short introduction for advanced undergraduate and beginning graduate students taking their first steps into EPR research.

There is a growing need in both industrial and academic research to obtain accurate quantitative results from continuous wave (CW) electron paramagnetic resonance (EPR) experiments. This book describes various sample-related, instrument-related and software-related aspects of obtaining quantitative results from EPR expe- ments. Some speci?c items to be discussed include: selection of a reference standard, resonator considerations (Q, B ,B ), power saturation, sample position- 1 m ing, and ?nally, the blending of all the factors together to provide a calculation model for obtaining an accurate spin concentration of a sample. This book might, at ?rst glance, appear to be a step back from some of the more advanced pulsed methods discussed in recent EPR texts, but actually quantitative “routine CW EPR” is a challenging technique, and requires a thorough understa- ing of the spectrometer and the spin system. Quantitation of CW EPR can be subdivided into two main categories: (1) intensity and (2) magnetic ?eld/mic- wave frequency measurement. Intensity is important for spin counting. Both re- tive intensity quantitation of EPR samples and their absolute spin concentration of samples are often of interest. This information is important for kinetics, mechanism elucidation, and commercial applications where EPR serves as a detection system for free radicals produced in an industrial process. It is also important for the study of magnetic properties. Magnetic ?eld/microwave frequency is important for g and nuclear hyper?ne coupling measurements that re?ect the electronic structure of the radicals or metal ions.

Although originally invented and employed by physicists, electron paramagnetic resonance (EPR) spectroscopy has proven to be a very efficient technique for studying a wide range of phenomena in many fields, such as chemistry, biochemistry, geology, archaeology, medicine, biotechnology, and environmental sciences. Acknowledging that not all studies require the same level of understanding of this technique, this book thus provides a practical treatise clearly oriented toward applications, which should be useful to students and researchers of various levels and disciplines. In this book, the principles of continuous wave EPR spectroscopy are progressively, but rigorously, introduced, with emphasis on interpretation of the collected spectra. Each chapter is followed by a section highlighting important points for applications, together with exercises solved at the end of the book. A glossary defines the main terms used in the book, and particular topics, whose knowledge is not required for understanding the main text, are developed in appendices for more inquisitive readers.

Instrumental techniques for analyzing intrinsically disordered proteins The recently recognized phenomenon of protein intrinsic disorder is gaining significant interest among researchers, especially as the number of proteins and protein domains that have been shown to be intrinsically disordered rapidly grows. The first reference to tackle this little-documented area, Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation provides researchers with a much-needed, comprehensive summary of recent achievements in the methods for structural characterization of intrinsically disordered proteins (IDPs). Chapters discuss: Assessment of IDPs in the living cell Spectroscopic techniques for the analysis of IDPs, including NMR and EPR spectroscopies, FTIR, circular dichroism, fluorescence spectroscopy, vibrational methods, and single-molecule analysis Single-molecule techniques applied to the study of IDPs Assessment of IDP size and shape Tools for the analysis of IDP conformational stability Mass spectrometry Approaches for expression and purification of IDPs With contributions from an international selection of leading researchers, Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation fills an important need in a rapidly growing field. It is required reading for biochemists, biophysicists, molecular biologists, geneticists, cell biologists, physiologists, and specialists in drug design and development, proteomics, and molecular medicine with an interest in proteins and peptides.

This book covers the basic theory and techniques, as well as various applications of pulsed electron–electron double resonance (PELDOR or DEER). This electron paramagnetic resonance technique is able to measure the distances and the distribution of distances between electron spins in the 1.5–15 nanometer scale; to determine the geometry of spin-labeled molecules; to estimate the number of interacting spins in spin clusters; and to characterize the spatial distribution of paramagnetic centers. As a result, PELDOR is now a popular method in EPR spectroscopy, particularly in the context of biologically important systems and soft matter and is also applied to problems in physical chemistry, biochemistry, polymers, soft matter and materials. Enabling readers to gain an understanding of the fundamentals of the PELDOR methods and an appreciation of the opportunities PELDOR provides, the book helps readers solve their own physical and biochemical problems.

High-Field EPR Spectroscopy on Proteins and their Model Systems: characterization of Transient Paramagnetic States offers a comprehensive overview of experimental techniques in, and paradigmatic examples of, the application of high-field EPR spectroscopy in biology and chemistry.