The volume presents a survey of the research by Kurt Wüthrich and his associates during the period 1965 to 1994. A selection of reprints of original papers on the use of NMR spectroscopy in structural biology is supplemented with an introduction, which outlines the foundations and the historical development of the use of NMR spectroscopy for the determination of three-dimensional structures of biological macromolecules in solution. The original papers are presented in groups highlighting protein structure determination by NMR, studies of dynamic properties and hydration of biological macromolecules, and practical applications of the NMR methodology in fields such as enzymology, transcriptional regulation, immunosuppression and protein folding.

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.

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.

To honour W C R”ntgen and review the entire area of X-ray development in the various fields of natural, technical, and life sciences, his successors at the Physikalisches Institut of the Universit„t Wrzburg organized a conference, named ?R”ntgen Centennial?. It took place at the new ?Physikalisches Institut? not far from the historical site shortly before the actual 100th anniversary of the discovery. Over forty renowned scientists were invited as representative speakers in the various subfields of X-ray activities. They reviewed the development, gave examples, and described the present status. Most of them provided survey articles, which are gathered in this book. Since most X-ray-related activities are somehow represented, an almost complete overview of the entire field is provided. This book thus represents the enormous breadth of X-ray activities and allows one to recognize the potential and quality of today's X-ray research.

This invaluable book comprises assorted recent papers of Professor C N R Rao, a well-known chemist. It presents current trends in materials chemistry and physics, offering in-depth information to young researchers and pleasant reading to experts. Advances in Chemistry brings out the single-minded dedication of Professor Rao to the promotion of science.

Lists of tables. The foundations: structure and NMR of biopolymers. Resonance assignments and structure determination in proteins. Resonance assignments and structure determiantion in nucleic acids. With NMR to biopolymer conformation and beyond.

This invaluable book distils the research accomplishments of Professor Fred Basolo during the five decades when he served as a world leader in the modern renaissance of inorganic chemistry. Its primary focus is on the very important area of chemistry known as coordination chemistry.Most of the elements in the periodic table are metals, and most of the chemistry of metals involves coordination chemistry. This is the case in the currently significant areas of research, including organometallic homogenous catalysis, biological reactions of metalloproteins, and even the solid state extended structures of new materials. In these systems, the metals are of primary importance because they are the sites of ligand substitution or redox reactions. In the solid materials, the coordination number of the metal and its stereochemistry are of major importance.Some fifty years of research on transition metal complexes carried out in the laboratory of Professor Basolo at Northwestern University is recorded here as selected scientific publications. The book is divided into three different major research areas, each dealing with some aspect of coordination chemistry. In each case, introductory remarks are presented which indicate what prompted the research projects and what the major accomplishments were. Although the research was of the academic, curiosity-driven type, some aspects have proven to be useful to others involved in projects that were much more applied in nature.

Linus Pauling wrote a stellar series of over 800 scientific papers spanning an amazing range of fields, some of which he himself initiated. This book is a selection of the most important of his writings in the fields of quantum mechanics, chemical bonding (covalent, ionic, metallic, and hydrogen bonding), molecular rotation and entropy, protein structure, hemoglobin, molecular disease, molecular evolution, the antibody mechanism, the molecular basis of anesthesia, orthomolecular medicine, radiation chemistry?biology, and nuclear structure. Through these papers the reader gets a fresh, unfiltered view of the genius of Pauling's many contributions to chemistry, chemical physics, molecular biology, and molecular medicine.

This book presents various computer-aided drug discovery methods for the design and development of ligand and structure-based drug molecules. A wide variety of computational approaches are now being used in various stages of drug discovery and development, as well as in clinical studies. Yet, despite the rapid advances in computer software and hardware, combined with the exponential growth in the available biological information, there are many challenges that still need to be addressed, as this book shows. In turn, it shares valuable insights into receptor-ligand interactions in connection with various biological functions and human diseases. The book discusses a wide range of phylogenetic methods and highlights the applications of Molecular Dynamics Simulation in the drug discovery process. It also explores the application of quantum mechanics in order to provide better accuracy when calculating protein-ligand binding interactions and predicting binding affinities. In closing, the book provides illustrative descriptions of major challenges associated with computer-aided drug discovery for the development of therapeutic drugs. Given its scope, it offers a valuable asset for life sciences researchers, medicinal chemists and bioinformaticians looking for the latest information on computer-aided methodologies for drug development, together with their applications in drug discovery.

This book discusses how biological molecules exert their function and regulate biological processes, with a clear focus on how conformational dynamics of proteins are critical in this respect. In the last decade, the advancements in computational biology, nuclear magnetic resonance including paramagnetic relaxation enhancement, and fluorescence-based ensemble/single-molecule techniques have shown that biological molecules (proteins, DNAs and RNAs) fluctuate under equilibrium conditions. The conformational and energetic spaces that these fluctuations explore likely contain active conformations that are critical for their function. More interestingly, these fluctuations can respond actively to external cues, which introduces layers of tight regulation on the biological processes that they dictate. A growing number of studies have suggested that conformational dynamics of proteins govern their role in regulating biological functions, examples of this regulation can be found in signal transduction, molecular recognition, apoptosis, protein / ion / other molecules translocation and gene expression. On the experimental side, the technical advances have offered deep insights into the conformational motions of a number of proteins. These studies greatly enrich our knowledge of the interplay between structure and function. On the theoretical side, novel approaches and detailed computational simulations have provided powerful tools in the study of enzyme catalysis, protein / drug design, protein / ion / other molecule translocation and protein folding/aggregation, to name but a few. This work contains detailed information, not only on the conformational motions of biological systems, but also on the potential governing forces of conformational dynamics (transient interactions, chemical and physical origins, thermodynamic properties). New developments in computational simulations will greatly enhance our understanding of how these molecules function in various biological events.