Protein research is a frontier field in science. Proteins are widely distributed in plants and animals and are the principal constituents of the protoplasm of all cells, and consist essentially of combinations of a-amino acids in peptide linkages. Twenty different amino acids are commonly found in proteins, and serve as enzymes, structural elements, hormones, immunoglobulins, etc., and are involved throughout the body, and in photosynthesis. This book gathers new leading-edge research from throughout the world in this exciting and exploding field of research.

Protein research is a frontier field in science. Proteins are widely distributed in plants and animals and are the principal constituents of the protoplasm of all cells, and consist essentially of combinations of a-amino acids in peptide linkages. Twenty different amino acids are commonly found in proteins, and serve as enzymes, structural elements, hormones, immunoglobulins, etc., and are involved throughout the body, and in photosynthesis. This book gathers new leading-edge research from throughout the world in this exciting and exploding field of research.

This work covers advances in the interactions of proteins with their solvent environment and provides fundamental physical information useful for the application of proteins in biotechnology and industrial processes. It discusses in detail structure, dynamic and thermodynamic aspects of protein hydration, as well as proteins in aqueous and organic solvents as they relate to protein function, stability and folding.

Although infrared spectroscopy has been applied with success to the study of important biological and biomedical processes for many years, key advances in this vibrant technique have led to its increasing use, ranging from characterization of individual macromolecules (DNA, RNA, lipids, proteins) to human tissues, cells and their components. Infrared spectroscopy thus has a significant role to play in the analysis of the vast number of genes and proteins being identified by the various genomic sequencing projects. Whilst this book gives an overview of the field, it highlights more recent developments, such as the use of bright synchrotron radiation for recording infrared spectra, the development of two-dimensional infrared spectroscopy and the ability to record infrared spectra at ultra fast speeds.

Presents a unified theoretical treatment, which is complete and rigorous but nonetheless readable. The theoretical treatment requires a variety of mathematical and physical tools. To keep the main text uncluttered, these tools are developed in comprehensive Appendices to which cross-references are made in the main text. These Appendices also ensure that the main text is useful to readers with a wide variety of scientific backgrounds and experience. These include not only spectroscopists, but also chemists, physicists, biochemists and analytical chemists. The presentation is such that postgraduate and postdoctoral students as well as more established research workers will find it valuable. About the Author The author was formerly Professor of Structural Chemistry and Director of the Molecular Spectroscopy unit in the University of Bradford. He is distinguished for his original scientific work in a number of areas of Raman spectroscopy. His book, 'Raman Spectroscopy', published in 1978 and long out of print, was highly successful. He has been co-editor of many books including the Specialist Reports on Molecular Spectroscopy, published by the Royal Society of Chemistry; he retired as Editor-in-Chief of the Journal of Raman Spectroscopy in December 1999.

This book provides an introduction to the important methods of chiroptical spectroscopy in general, and circular dichroism (CD) in particular, which are increasingly important in all areas of chemistry, biochemistry, and structural biology. The book can be used as a text for undergraduate and graduate students and as a reference for researchers in academia and industry. Experimental methods and instrumentation are described with topics ranging from the most widely used methods (electronic and vibrational CD) to frontier areas such as nonlinear spectroscopy and photoelectron CD, as well as the theory of chiroptical methods and techniques for simulating chiroptical properties. Applications of chiroptical spectroscopy to problems in organic stereochemistry, inorganic stereochemistry, and biochemistry and structural biology are also discussed, and each chapter is written by one or more leading authorities with extensive experience in the field.

This second, thoroughly revised, updated and enlarged edition provides a straightforward introduction to spectroscopy, showing what it can do and how it does it, together with a clear, integrated and objective account of the wealth of information that may be derived from spectra. It also features new chapters on spectroscopy in nano-dimensions, nano-optics, and polymer analysis. Clearly structured into sixteen sections, it covers everything from spectroscopy in nanodimensions to medicinal applications, spanning a wide range of the electromagnetic spectrum and the physical processes involved, from nuclear phenomena to molecular rotation processes. In addition, data tables provide a comparison of different methods in a standardized form, allowing readers to save valuable time in the decision process by avoiding wrong turns, and also help in selecting the instrumentation and performing the experiments. These four volumes are a must-have companion for daily use in every lab.

The subject of this book is the amazing enzyme ribonucleotide reductase (RNR), the enzyme responsible for the conversion of ribonucleotides to deoxyribonucleotides. The prerequisite for DNA-synthesis and DNA-repair in all living cells is the supply of the four deoxyribonucleotides. Such molecules result from the enzymatically difficult radical-induced reduction of ribonucleotides, a multistep chemical process catalyzed by RNR. RNR was the first enzyme in which the presence of an amino acid radical (a tyrosyl) in E. coli Class Ia RNR has been proven; since then several other biological amino acid radical species have been found on e.g. tryptophan, glycine, cysteine, lysine residues and on amino acid derived small cofactors like 2 tryptophanes in thryptophan-trypthanyl-radical or cysteine-tyrosyl-radical in other enzymes. As all known cellular life forms store their genetic information as DNA, RNR is likely to be found in all growing cells of every living organism, a fact that is confirmed by a rapidly increasing number of genomic screenings.

This book discusses biomedical spectroscopy and the applications of spectroscopic techniques in advanced medical technology. Applicable to scientists and medical professionals, the aim of this work is to enable them to work together in this field, so that healthcare facilities can be made routinely available in a cost-effective manner—especially for developing countries which may not be able to afford universal healthcare with present day expensive medical technologies. The subject matter of this book also covers – Instrumentation, Experimental Techniques and Computational Methods Spectroscopy of Animal Models Microspectroscopy for Biomedical Applications Clinical Applications of Optical Spectroscopy Spectroscopy of Human Models Print edition not for sale in South Asia (India, Sri Lanka, Nepal, Bangladesh, Pakistan and Bhutan)

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.