NMR spectroscopy has found a wide range of applications in life sciences over recent decades. Providing a comprehensive amalgamation of the scattered knowledge of how to apply high-resolution NMR techniques to biomolecular systems, this book will break down the conventional stereotypes in the use of NMR for structural studies. The major focus is on novel approaches in NMR which deal with the functional interface of either protein-protein interactions or protein-lipid interactions. Bridging the gaps between structural and functional studies, the Editors believe a thorough compilation of these studies will open an entirely new dimension of understanding of crucial functional motifs. This in turn will be helpful for future applications into drug design or better understanding of systems. The book will appeal to NMR practitioners in industry and academia who are looking for a comprehensive understanding of the possibilities of applying high-resolution NMR spectroscopic techniques in probing biomolecular interactions.
This book presents a critical assessment of progress on the use of nuclear magnetic resonance spectroscopy to determine the structure of proteins, including brief reviews of the history of the field along with coverage of current clinical and in vivo applications. The book, in honor of Oleg Jardetsky, one of the pioneers of the field, is edited by two of the most highly respected investigators using NMR, and features contributions by most of the leading workers in the field. It will be valued as a landmark publication that presents the state-of-the-art perspectives regarding one of today's most important technologies.
Modern research in biology increasingly relies on multiple techniques for describing structures and mechanisms. This book provides an overview of the contemporary integrated biology approaches for solving structures and understanding mechanisms of complex biological systems. It includes several methodology chapters discussing the current developments in the areas of cryo-electron microscopy (EM) and cryo-electron tomography (ET), computational biophysics, solution NMR spectroscopy, solid-state NMR spectroscopy and dynamic nuclear polarization (DNP), electron paramagnetic resonance (EPR), (photo-)chemically induced dynamic nuclear polarization (CIDNP), X-ray crystallography and small-angle X-ray and neutron scattering (SAXS/SANS). Several subsequent chapters demonstrate how these methods are used in synergy to address problems at the forefront of structural biology, with particular emphasis on examples where individual techniques are insufficient. Examples of biological systems include membrane proteins, viral protein assemblies, cytoskeleton protein assemblies, photosynthetic reaction centers, large enzyme complexes and whole cells. The book is targeted to both the current practitioners of structural biology and scientists who are interested in entering the fields of structural biology or biophysical chemistry.
How can we study one of the most elusive molecular properties, chirality, using nuclear interactions with the magnetic field that are apparently insensitive to handedness? This book answers this question from the physicochemical point of view by providing a clear, coherent, and comprehensive review of methods used in NMR studies of chirality. Presented arguments based on fundamental physical and chemical laws and in-depth descriptions of new methods utilizing purely physical interactions are mainly addressed to spectroscopists in both academia and industry. The introductory chapters provide the reader with the basics of NMR spectroscopy as a tool for the study of chiral compounds, and those more interested in the methods of chiral discrimination will benefit from the brief description of their common points and reasons why some of them may or may not work. In the following chapters, the book shows rapid progress in a newly emerging field of chirality-sensitive NMR, in particular, a search for effects that give direct information about the absolute configuration of a molecule.
TWO-DIMENSIONAL (2D) NMR METHODS Practical guide explaining the fundamentals of 2D-NMR for experienced scientists as well as relevant for advanced students Two-Dimensional (2D) NMR Methods is a focused work presenting an overview of 2D-NMR concepts and techniques, including basic principles, practical applications, and how NMR pulse sequences work. Contributed to by global experts with extensive experience in the field, Two-Dimensional (2D) NMR Methods provides in-depth coverage of sample topics such as: Basics of 2D-NMR, data processing methods (Fourier and beyond), product operator formalism, basics of spin relaxation, and coherence transfer pathways Multidimensional methods (single- and multiple-quantum spectroscopy), NOESY (principles and applications), and DOSY methods Multiple acquisition strategies, anisotropic NMR in molecular analysis, ultrafast 2D methods, and multidimensional methods in bio-NMR TROSY (principles and applications), field-cycling and 2D NMR, multidimensional methods and paramagnetic NMR, and relaxation dispersion experiments This text is a highly useful resource for NMR specialists and advanced students studying NMR, along with users in research, academic and commercial laboratories that study or conduct experiments in NMR.
Molecular chaperones are critical to control protein quality in all living cells. Understanding chaperone function at the atomic level, and in particular its mode of interaction with client proteins, is crucial to understanding the fundamental roles chaperones play in biology. This book fills a gap in the literature by comprehensively summarizing and discussing new advanced experimental techniques for their analysis. Providing a comprehensive overview of advanced biophysical methods for the characterization of molecular mechanisms of molecular chaperones, the majority of the contributions are NMR methodology. This is the method of choice for atomic resolution studies of such systems. Additional notable biophysical approaches are considered to present all relevant current developments in exploring chaperone function and the transient and dynamic interactions with their client proteins. The book is targeted at both current practitioners of structural biology and biophysical chemistry and scientists who are interested in entering the field. It could be useful for graduate students as supplementary reading.
Global climate change is the most important challenge humankind is facing in the modern era. One of the main scientific concerns is the monitoring of contaminants in the environment, which require the right environmental remediation strategies. In this context, nuclear magnetic resonance (NMR) techniques have a very important role in enabling the discovery of how pollutants are transformed, how they can move and how they can affect human health. This book discusses the present and the future perspectives of NMR techniques for environmental evaluations. It covers, amongst other topics, the importance of NMR as a contamination discovery tool, how to improve sensitivity in environmental NMR, and multiphase NMR for measurement of samples in their natural state. Samples include lubricant oils, soils and porous media. Due to the direct relationship between the environment and human health, there is information dedicated to the use of magnetic resonance imaging (MRI) to monitor human health as related to environmental pollution. There is also a chapter on how NMR is used in cultural heritage to measure artefacts directly affected by environmental pollution. Filling a gap in the literature, the book is for researchers explaining how to apply their knowledge of NMR techniques to solve environmental problems, and for students who want to deepen their understanding of this topic.
Residual dipolar couplings (RDCs) are NMR measurements widely used to determine structural and dynamic information in small molecules and large macromolecules. This book provides a broad view of RDCs, from basic principles to advanced applications in organic molecules and biomolecules. Exploring the newest developments in RDC measurement and analysis through authoritative accounts written by leaders in the field, this book provides a comprehensive overview on the fundamentals, analysis and applications in one place for the first time. The versatility and accuracy of RDCs have found a large range of applications in NMR, and their measurement and analysis are major research areas. Readers, be they experts or students, will receive a strong understanding of the fundamentals of RDCs and their applications to their research projects.
This book describes recent important advancements in protein folding dynamics and stability research, as well as explaining fundamentals and examining potential methodological approaches in protein science. In vitro, in silico, and in vivo method based research of how the stability and folding of proteins help regulate the cellular dynamics and impact cell function that are crucial in explaining various physiological and pathological processes. This book offers a comprehensive coverage on various techniques and related recent developments in the experimental and computational methods of protein folding, dynamics, and stability studies. The book is also structured in such a way as to summarize the latest developments in the fiddle and key concepts to ensure that readers can understand advanced concepts as well as the fundamental big picture. And most of all, fresh insights are provided into the convergence of protein science and technology. Protein Folding Dynamics and Stability is an ideal guide to the field that will be of value for all levels of researchers and advanced graduate students with training in biochemical laboratory research.
This textbook provides an introduction to the fundamental and applied aspects of biophysics for advanced undergraduate and graduate students of physics, chemistry, and biology. The application of physics principles and techniques in exploring biological systems has long been a tradition in scientific research. Biological systems hold naturally inbuilt physical principles and processes which are popularly explored. Systematic discoveries help us understand the structures and functions of individual biomolecules, biomolecular systems, cells, organelles, tissues, and even the physiological systems of animals and plants. Utilizing a physics- based scientific understanding of biological systems to explore disease is at the forefront of applied scientific research. This textbook covers key breakthroughs in biophysics whilst looking ahead to future horizons and directions of research. It contains models based on both classical and quantum mechanical treatments of biological systems. It explores diseases related to physical alterations in biomolecular structures and organizations alongside drug discovery strategies. It also discusses the cutting- edge applications of nanotechnologies in manipulating nanoprocesses in biological systems. Key Features: • Presents an accessible introduction to how physics principles and techniques can be used to understand biological and biochemical systems. • Addresses natural processes, mutations, and their purposeful manipulation. • Lays the groundwork for vitally important natural scientific, technological, and medical advances. Mohammad Ashrafuzzaman, a biophysicist and condensed matter scientist, is passionate about investigating biological and biochemical processes utilizing physics principles and techniques. He is a professor of biophysics at King Saud University’s Biochemistry Department in the College of Science, Riyadh, Saudi Arabia; the co- founder of MDT Canada Inc., and the founder of Child Life Development Institute, Edmonton, Canada. He has authored Biophysics and Nanotechnology of Ion Channels, Nanoscale Biophysics of the Cell, and Membrane Biophysics. He has also published about 50 peer- reviewed articles and several patents, edited two books, and has been serving on the editorial boards of Elsevier and Bentham Science journals. Dr. Ashrafuzzaman has held research and academic ranks at Bangladesh University of Engineering & Technology, University of Neuchatel (Switzerland), Helsinki University of Technology (Finland), Weill Medical College of Cornell University (USA), and University of Alberta (Canada). During 2013– 2018 he also served as a Visiting Professor at the Departments of Oncology, and Medical Microbiology and Immunology, of the University of Alberta. Dr. Ashrafuzzaman earned his highest academic degree, Doctor of Science (D.Sc.) in condensed matter physics from the University of Neuchatel, Switzerland in 2004.
