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Written by one of the most significant contributors to the progress of protein crystallography, this practical guide contains case studies, a troubleshooting section and pointers on data interpretation. It covers the theory, practice and latest achievements in x-ray crystallography, such that any researcher in structural biology will benefit from this extremely clearly written book. Part A covers the theoretical basis and such experimental techniques as principles of x-ray diffraction, solutions for the phase problem and time-resolved x-ray crystallography. Part B includes case studies for different kinds of x-ray crystal structure determination, such as the MIRAS and MAD techniques, molecular replacement, and the difference Fourier technique.
This book provides an integrated treatment of the structure and function of nucleic acids, proteins, and glycans, including thorough coverage of relevant computational biochemistry. The text begins with an introduction to the biomacromolecules, followed by discussion of methods of isolation and purification, physiochemical and biochemical properties, and structural characteristics. The next section of the book deals with sequence analysis, analysis of conformation using spectroscopy, chemical synthesis, and computational approaches. The following chapters discuss biomolecular interactions, enzyme action, gene transmission, signal transduction, and biomacromolecular informatics. The author concludes with presenting the latest findings in genomics, proteomics, glycomics, and biomacromolecular evolution. This text is an invaluable resource for research professionals wishing to move into genomics, proteomics, and glycomics research. It is also useful for students in biochemistry, molecular biology, bioengineering, biotechnology, and bioinformatics.
Crystallography Made Crystal Clear is designed to meet the need for an X-ray analysis that is between brief textbook sections and complete treatments. The book provides non-crystallographers with an intellectually satisfying explanation of the principles of how protein models are gleaned from X-ray analysis. The understanding of these concepts will foster wise use of the models, including the recognition of the strengths and weaknesses of pictures or computer graphics. Since proteins comprise the majority of the mass of macromolecules in cells and carry out biologically important tasks, the book will be of interest to biologists.Provides accessible descriptions of principles of x-ray crystallography, built on simple foundations for anyone with a basic science backgroundLeads the reader through clear, thorough, unintimidating explanations of the mathematics behind crystallographyExplains how to read crystallography papers in research journalsIf you use computer-generated models of proteins or nucleic acids for:Studying molecular interactionsDesigning ligands, inhibitors, or drugsEngineering new protein functionsInterpreting chemical, kinetic, thermodynamic, or spectroscopic dataStudying protein foldingTeaching macromolecule structure,and if you want to read new structure papers intelligently; become a wiser user of macromolecular models; and want to introduce undergraduates to the important subject of x-ray crystallography, then this book is for you.
Applications of nuclear magnetic resonance span a wide range of scientific disciplines, from physics to medicine. This series has provided an essential digest of the NMR literature for more than four decades and each volume provides unrivalled coverage of the literature on this topic. Continuous coverage on some topics such as theoretical and physical aspects of nuclear shielding is balanced by the desire for coverage on newer topics like applications in biological systems and materials science. For those wanting to become rapidly acquainted with NMR or seasoned practitioners, this is an invaluable source of current methods and applications.
The book describes the individual steps necessary for biomacromolecular fragments analysis, as well as a list of essential software tools. For each step, it also shows corresponding web-based tools in detail and provides practical examples of their use. All tools and databases mentioned in the examples are available free of charge, platform-independent, web-based, user-friendly and do not require a prior IT background to be fully used.
Biology has entered an era in which interdisciplinary cooperation is at an all-time high, practical applications follow basic discoveries more quickly than ever before, and new technologiesâ€"recombinant DNA, scanning tunneling microscopes, and moreâ€"are revolutionizing the way science is conducted. The potential for scientific breakthroughs with significant implications for society has never been greater. Opportunities in Biology reports on the state of the new biology, taking a detailed look at the disciplines of biology; examining the advances made in medicine, agriculture, and other fields; and pointing out promising research opportunities. Authored by an expert panel representing a variety of viewpoints, this volume also offers recommendations on how to meet the infrastructure needsâ€"for funding, effective information systems, and other supportâ€"of future biology research. Exploring what has been accomplished and what is on the horizon, Opportunities in Biology is an indispensable resource for students, teachers, and researchers in all subdisciplines of biology as well as for research administrators and those in funding agencies.
The volume is intended as an introduction to the physical principles governing the main processes that occur in photosynthesis, with emphasis on the light reactions and electron transport chain. A unique feature of the photosynthetic apparatus is the fact that the molecular structures are known in detail for essentially all of its major components. The availability of this data has allowed their functions to be probed at a very fundamental level to discover the design principles that have guided evolution. Other volumes on photosynthesis have tended to focus on single components or on a specific set of biophysical techniques, and the authors’ goal is to provide new researchers with an introduction to the overall field of photosynthesis. The book is divided into sections, each dealing with one of the main physical processes in photosynthetic energy conversion. Each section has several chapters each describing the role that a basic physical property, such as charge or spin, plays in governing the process being discussed. The chapters proceed in an orderly fashion from a quantum mechanical description of early processes on an ultrafast timescale to a classical treatment of electron transfer and catalysis on a biochemical timescale culminating in evolutionary principles on a geological timescale.
This book describes the advanced developments in methodology and applications of NMR spectroscopy to life science and materials science. Experts who are leaders in the development of new methods and applications of life and material sciences have contributed an exciting range of topics that cover recent advances in structural determination of biological and material molecules, dynamic aspects of biological and material molecules, and development of novel NMR techniques, including resolution and sensitivity enhancement. First, this book particularly emphasizes the experimental details for new researchers to use NMR spectroscopy and pick up the potentials of NMR spectroscopy. Second, the book is designed for those who are involved in either developing the technique or expanding the NMR application fields by applying them to specific samples. Third, the Nuclear Magnetic Resonance Society of Japan has organized this book not only for NMR members of Japan but also for readers worldwide who are interested in using NMR spectroscopy extensively.
Protein NMR Spectroscopy, Second Edition combines a comprehensive theoretical treatment of NMR spectroscopy with an extensive exposition of the experimental techniques applicable to proteins and other biological macromolecules in solution. Beginning with simple theoretical models and experimental techniques, the book develops the complete repertoire of theoretical principles and experimental techniques necessary for understanding and implementing the most sophisticated NMR experiments. Important new techniques and applications of NMR spectroscopy have emerged since the first edition of this extremely successful book was published in 1996. This updated version includes new sections describing measurement and use of residual dipolar coupling constants for structure determination, TROSY and deuterium labeling for application to large macromolecules, and experimental techniques for characterizing conformational dynamics. In addition, the treatments of instrumentation and signal acquisition, field gradients, multidimensional spectroscopy, and structure calculation are updated and enhanced. The book is written as a graduate-level textbook and will be of interest to biochemists, chemists, biophysicists, and structural biologists who utilize NMR spectroscopy or wish to understand the latest developments in this field. - Provides an understanding of the theoretical principles important for biological NMR spectroscopy - Demonstrates how to implement, optimize and troubleshoot modern multi-dimensional NMR experiments - Allows for the capability of designing effective experimental protocols for investigations of protein structures and dynamics - Includes a comprehensive set of example NMR spectra of ubiquitin provides a reference for validation of experimental methods