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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.
The book provides insights into the research of the Kurt Wüthrich laboratories from 1996-2020. During this time period, the technique of nuclear magnetic resonance (NMR) spectroscopy in solution went through several breakthroughs, while maturing into a standard method of structural biology. With the introduction of TROSY (transverse relaxation-optimized spectroscopy), the range of accessible molecular sizes was extended about thirty-fold, and efficient protein structure determination resulted from the demands of the structural genomics initiative. Applications in fundamental biology and biomedicine include studies of prion proteins and prion diseases (TSEs), the SARS-Corona virus proteome, trans-membrane signalling by G protein-coupled receptors (GPCRs), and signal transfer by pheromones.Key publications from the Kurt Wüthrich laboratories are placed in perspective, providing insights into new aspects of NMR spectroscopy in structural biology. In addition to methods development, this includes applications in diverse areas of biological research, such as prion proteins and their role in transmissible spongiform encephalopathies (TSEs), trans-membrane signal transfer by G protein-coupled receptors (GPCRs), structural characterization of the SARS-Corona virus proteome, metabolic-flux profiling in bacterial cultures, and signal transfers by pheromones.
An Introduction that describes the origin of cytochrome notation also connects to the history of the field, focusing on research in England in the pre-World War II era. The start of the modern era of studies on structure-function of cytochromes and energy-transducing membrane proteins was marked by the 1988 Nobel Prize in Chemistry, given to J. Deisenhofer, H. Michel, and R. Huber for determination of the crystal structure of the bacterial photosynthetic reaction center. An ab initio logic of presentation in the book discusses the evolution of cytochromes and hemes, followed by theoretical perspectives on electron transfer in proteins and specifically in cytochromes. There is an extensive description of the molecular structures of cytochromes and cytochrome complexes from eukaryotic and prokaryotic sources, bacterial, plant and animal. The presentation of atomic structure information has a major role in these discussions, and makes an important contribution to the broad field of membrane protein structure-function.
Membrane bioenergetics is one of the most rapidly growing areas within physico-chemical biology. Main aspects treated in this book include energy conservation and utilization by membrane-linked molecular mechanisms such as intracellular respiration, photosynthesis, transport phenomena, rotation of bacterial flagella, and the regulation of heat production.