Infrared radiation (IR) analysis is proving a powerful tool for understanding the structure and function of peptides and proteins, but the method remains relatively little known. This book examines these applications in detail, providing a valuable source for both basic methods and new refinements.
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.
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.
Infrared and Raman Spectroscopy of Biological Materials facilitates a comprehensive and through understanding of the latest developments in vibrational spectroscopy. It contains explains key breakthroughs in the methodologies and techniques for infrared, near-infrared, and Raman spectroscopy. Topics include qualitative and quantitative analysis, biomedical applications, vibrational studies of enzymatic catalysis, and chemometrics.
This book is not intended to be a basic text in infrared spectroscopy. Many such books exist and I have referred to them in the text. Rather, I have tried to find applications that would be interesting to a variety of people: advanced undergraduate chemistry students, graduate students and research workers in several disciplines, spectros copists, and physicians active in research or in the practice of medicine. With this aim in mind there was no intent to have exhaustive coverage of the literature. I should like to acknowledge my use of several books and reviews, which were invaluable in my search for material: G. H. Beaven, E. A. Johnson, H. A. Willis and R. G. 1. Miller, Molecular Spec troscopy, Heywood and Company, Ltd., London, 1961. J. A. Schell man and Charlotte Schellman, 'The Conformation of Polypeptide Chains in Proteins," in The Proteins, Vol. II, 2nd Ed. (H. Neurath, ed.), Academic Press, New York, 1964. R. T. O'Connor, "Application of Infrared Spectrophotometry to Fatty Acid Derivatives," J. Am. Oil Chemists' Soc. 33, 1 (1956). F. L. Kauffman, "Infrared Spectroscopy of Fats and Oils," J. Am. Oil Chemists' Soc. 41,4 (1964). W. J. Potts, Jr., Chemical Infrared Spectroscopy, Vol. I, Techniques, Wiley, New York, 1963. R. S. Tipson, Infrared Spectroscopy of Carbohydrates, National Bureau of Standards Monograph llO, Washington, D.C., 1968. C. N. R. Rao, Chemical Applications of Infrared Spectroscopy, Academic Press, New York, 1963.
2D infrared (IR) spectroscopy is a cutting-edge technique, with applications in subjects as diverse as the energy sciences, biophysics and physical chemistry. This book introduces the essential concepts of 2D IR spectroscopy step-by-step to build an intuitive and in-depth understanding of the method. This unique book introduces the mathematical formalism in a simple manner, examines the design considerations for implementing the methods in the laboratory, and contains working computer code to simulate 2D IR spectra and exercises to illustrate involved concepts. Readers will learn how to accurately interpret 2D IR spectra, design their own spectrometer and invent their own pulse sequences. It is an excellent starting point for graduate students and researchers new to this exciting field. Computer codes and answers to the exercises can be downloaded from the authors' website, available at www.cambridge.org/9781107000056.
Furthering efforts to simulate the potency and specificity exhibited by peptides and proteins in healthy cells, this remarkable reference supplies pharmaceutical scientists with a wealth of techniques for tapping the enormous therapeutic potential of these molecules-providing a solid basis of knowledge for new drug design. Provides a broad, comprehensive overview of peptides and proteins as mediators of cell movement, proliferation, differentiation, and communication. Written by more than 50 leading international authorities, Peptides and Protein Drug Analysis discusses strategies for dealing with the complexity of peptides and proteins in conformational flexibility and amino acid sequence variability analyzes drug formulations facilitated by solid-phase peptide synthesis and recombinant DNA technology examines chemical purity analysis by high-pressure chromatographic, capillary electrophoretic, gel electrophoretic, and isoelectric focusing methods highlights drug design elements derived from protein folding, bioinformatics, and computational chemistry demonstrates uses of unnatural mutagenesis and combinatorial chemistry explores mass spectrometry, protein sequence, and carbohydrate analysis illustrates bioassays and other new functional analysis methods surveys spectroscopic techniques such as ultraviolet, fluorescence, Fourier transform infrared, and nuclear magnetic resonance (NMR) addresses ways of distinguishing between levels of therapeutic and endogenous agents in cells reviews structural analysis tools such as ultracentrifugation and light, X-ray, and neutron scattering and more! Featuring over 3400 bibliographic citations and more than 500 tables, equations, and illustrations, Peptide and Protein Drug Analysis is a must-read resource for pharmacists; pharmacologists; analytical, organic, and pharmaceutical chemists; cell and molecular biologists; biochemists; and upper-level undergraduate and graduate students in these disciplines.
This book provides knowledge of the basic theory, spectral analysis methods, chemometrics, instrumentation, and applications of near-infrared (NIR) spectroscopy—not as a handbook but rather as a sourcebook of NIR spectroscopy. Thus, some emphasis is placed on the description of basic knowledge that is important in learning and using NIR spectroscopy. The book also deals with applications for a variety of research fields that are very useful for a wide range of readers from graduate students to scientists and engineers in both academia and industry. For readers who are novices in NIR spectroscopy, this book provides a good introduction, and for those who already are familiar with the field it affords an excellent means of strengthening their knowledge about NIR spectroscopy and keeping abreast of recent developments.
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.
A bestselling classic reference, now expanded and updated to cover the latest instrumentation, methods, and applications The Second Edition of Fourier Transform Infrared Spectrometry brings this core reference up to date on the uses of FT-IR spectrometers today. The book starts with an in-depth description of the theory and current instrumentation of FT-IR spectrometry, with full chapters devoted to signal-to-noise ratio and photometric accuracy. Many diverse types of sampling techniques and data processing routines, most of which can be performed on even the less expensive instruments, are then described. Extensively updated, the Second Edition: * Discusses improvements in optical components * Features a full chapter on FT Raman Spectrometry * Contains new chapters that focus on different ways of measuring spectra by FT-IR spectrometry, including fourteen chapters on such techniques as microspectroscopy, internal and external reflection, and emission and photoacoustic spectrometry * Includes a new chapter introducing the theory of vibrational spectrometry * Organizes material according to sampling techniques Designed to help practitioners using FT-IR capitalize on the plethora of techniques for modern FT-IR spectrometry and plan their experimental procedures correctly, this is a practical, hands-on reference for chemists and analysts. It's also a great resource for students who need to understand the theory, instrumentation, and applications of FT-IR.