SERIES IN STRUCTURAL BIOLOGY – serie

Several years ago, Thomas Steitz agreed to contribute a volume to the "World Scientific Series in Structural Biology" that would deal with the contributions he and his coworkers have made to structural biology during his remarkable career. Sadly, Tom died in the fall of 2018 before he had had time to do more than produce an outline for this book, and a list of the reprints he wanted it to contain.Fortunately, Tom's colleagues and coworkers responded enthusiastically when they were informed later that fall that if they were willing to help out, a volume would be published to commemorate his career. It fell to Anders Liljas, Peggy Eatherton, Tom's longtime administrative assistant, and Peter Moore, a close colleague, to oversee their efforts. Thomas Steitz is best known for the work he and his coworkers did to elucidate the biochemical basis of gene expression. The structures of a large number of the macromolecules involved in transcription and translation emerged from his laboratory over the course of his career. This book includes reprints of the most important papers he had published, grouped according to the structures they relate to, and commentaries written by the scientists who collaborated with him to solve each of them. It thus summarizes the achievements of one of the most distinguished biochemists of the second half of the 20th century.

This book describes the accomplishments of a curious and imaginative scientist, and his endeavours to translate or even to extrapolate scientific insights into the world of art.The science section in this volume concerns studies on S-layers, a very important class of proteins found on the surface of numerous Bacteria and nearly all Archaea. S-layer proteins are one of the most abundant biopolymers on our planet, and assemble into the simplest type of biological membrane. Moreover, they are unique building blocks and patterning elements for the production of complex supramolecular structures and nanoscale devices in nanobiotechnology, molecular nanotechnology, synthetic biology, biomimetics and nanomedicine.In the second part of this book the author goes on to passionately describe how his scientific activities stimulated his art work, which in particular concerns the visualization of results and the potential of synthetic biology and evolutionary events induced by genetic manipulations. Most importantly, the engagement in art allowed him to leave the rather curtailed canon of science and reach a mental state of unlimited freedom of thoughts. Mask-like sculptures are used as examples to visualize the intersection between science and art, and in particular the unpredictability and mystery of scientific visions.

This book provides a comprehensive coverage of the basic principles of structural biology, as well as an up-to-date summary of some main directions of research in the field. The relationship between structure and function is described in detail for soluble proteins, membrane proteins, membranes, and nucleic acids.There are several books covering protein structure and function, but none that give a complete picture, including nucleic acids, lipids, membranes and carbohydrates, all being of central importance in structural biology.The book covers state-of-the-art research in various areas. It is unique for its breadth of coverage by experts in the fields. The book is richly illustrated with more than 400 color figures to highlight the wide range of structures.

This book provides a comprehensive coverage of the basic principles of structural biology, as well as an up-to-date summary of some main directions of research in the field. The relationship between structure and function is described in detail for soluble proteins, membrane proteins, membranes, and nucleic acids.There are several books covering protein structure and function, but none that give a complete picture, including nucleic acids, lipids, membranes and carbohydrates, all being of central importance in structural biology.The book covers state-of-the-art research in various areas. It is unique for its breadth of coverage by experts in the fields. The book is richly illustrated with more than 400 color figures to highlight the wide range of structures.

This book is a guide for advanced undergraduates, post-graduates and researchers to the fundamental principles in studying kinetics and mechanism of processes concerning proteins. It provides a rare broad overview that concentrates on fundamental principles and understanding underlying the physics and chemistry. It is a single author text by someone who has direct experience in all of the areas covered.

This book is a guide for advanced undergraduates, post-graduates and researchers to the fundamental principles in studying kinetics and mechanism of processes concerning proteins. It provides a rare broad overview that concentrates on fundamental principles and understanding underlying the physics and chemistry. It is a single author text by someone who has direct experience in all of the areas covered.

The book reproduces 55 of more than 300 articles written by the author, representing milestones in methods development of single-particle cryo-EM as well as important results obtained by this technique in the study of biological macromolecules and their interactions. Importantly, neither symmetries nor ordered arrangements (as in two-dimensional crystals, helical assemblies, icosahedral viruses) are required. Although the biological applications are mainly in the area of ribosome structure and function, the elucidation of membrane channel structures and their activation and gating mechanisms are represented, as well. The book is introduced by a commentary that explains the original development of concepts, describes the contributions of the author's colleagues and students, and shows how challenges were overcome as the technique matured. Along the way, the ribosome served as an example for a macromolecule with intricate structure and conformational dynamics that pose challenges for three-dimensional visualization. Toward the end of the book — bringing us to the present time — molecular structures with near-atomic resolution are presented, and a novel type of computational analysis, manifold embedding, is introduced.Single-particle cryo-EM is currently revolutionizing structural biology, presenting a powerful alternative to X-ray crystallography as a means to solve the structure of biological macromolecules. The book presents in one place a number of articles containing key advances in mathematical and computational methods leading up to the present time. Secondly, the development of the technique over the years is reflected by ever-expanding discoveries in the field of ribosome structure and function. Thirdly, as all histories of ideas, the history of concepts pertaining to this new method of visualization is fascinating all in itself.

"This book brings back memories of the great Alex Rich, a pioneer in molecular biology. He was friend, a mentor and a colleague who contributed greatly to the understanding of living processes and molecular structures."David Baltimore1975 Nobel Laureate in Physiology or MedicineThis book is intended for students and general readers who are interested in the structures of biological molecules and history of science. The center of gravity of Alexander Rich's work is on nucleic acids and their structures and their roles in biology, but the breadth of his work is nearly unparalleled. Alex Rich published important early discoveries on the structure and activity of RNA, information transfer (translation) from RNA to protein, the structure of ribosomes with insights into polyribosome functions, the first atomic-resolution structure of nucleic acid base pairings, and the discovery of a hitherto-unknown conformation of DNA. Many of Rich's articles also have a focus on the structure of proteins in general as well as specific proteins and some are concerned with the structure of viruses. Some of Rich's early experimental work is based on scattering of X-rays from fibers but X-ray diffraction from crystals became the dominating technique of the Cold War.This is a book full of rich history of early days of modern biology and many fundamental discoveries. Alex Rich's main focus throughout his long career was on nucleic acids. His first paper on nucleic acids, was published together with JD Watson. Two years later, Rich reported creating fibers of poly-Uracil and poly-Adenine and studied their structures by diffraction.Alex Rich's laboratory determined the high resolution crystal structures of the ApU and GpC fragments of double helical RNA from Rich's group is considered a landmark in the detailed understanding of nucleic acid structure.

This highly illustrated book provides an up-to-date description of the structure and function of the translation system including ribosomes, tRNAs, translation factors, antibiotics and aminoacyl-tRNA synthetases.Research on translation is undergoing rapid changes and is receiving significant attention as evidenced by the Nobel Prize in Chemistry 2009. The structural research by crystallography and cryo-EM forms part of an interactive framework that involves biochemistry and molecular computation. The book provides a comprehensive overview of translation in light of the structural results. It is a valuable resource for scientists in this and related fields, as well as for students taking courses with a focus on translation.There is no other book in this field currently except the previous edition of this book. The authors have for a long time worked in the field of structure and function of the translation system.

This highly illustrated book provides an up-to-date description of the structure and function of the translation system including ribosomes, tRNAs, translation factors, antibiotics and aminoacyl-tRNA synthetases.Research on translation is undergoing rapid changes and is receiving significant attention as evidenced by the Nobel Prize in Chemistry 2009. The structural research by crystallography and cryo-EM forms part of an interactive framework that involves biochemistry and molecular computation. The book provides a comprehensive overview of translation in light of the structural results. It is a valuable resource for scientists in this and related fields, as well as for students taking courses with a focus on translation.There is no other book in this field currently except the previous edition of this book. The authors have for a long time worked in the field of structure and function of the translation system.

The book provides a synthetic and exhaustive view of how proteins have evolved their structure to accommodate a variety of metal ions in order to accomplish the most demanding chemical reactions that sustain life. This book may be the subject of a monographic course on its own or may complement bioinorganic chemistry textbooks to obtain a comprehensive view of the structural aspects of this subject. It is directed at advanced undergraduate and graduate students, researchers, instructors, and professors teaching in protein science, biochemistry, cell biology.This is the first textbook focused on 3D-structures of metalloproteins. It is also a tool for a monographic course on one or more biogeochemical cycles of metal ions. It provides a comprehensive overview of the structural chemistry of metal ions in proteins.

About 50 publications out of more than 500 have been selected from the work of Michael Rossmann covering the years from 1958 to 2012. These include his early work with Max Perutz on hemoglobin and the first protein structures to his current work on the structures of small icosahedral and large polymorphic viruses. These papers describe not only some of the first protein and virus structures, but also the crystallographic and electron microscopic technologies. Furthermore, the author's interests include evolution and protein folding.The selected papers are a personal history of structural biology and especially of structural virology. The papers describe many of the basic techniques of structural biology such as isomorphous replacement, anomalous dispersion of X-rays, the molecular replacement method, X-ray diffraction data processing and combining crystallographic data with electron microscopic images.The book covers much of the historical development of the modern flourishing field of structural biology in terms of the authors' own contributions.

The aim of this book is to make available, to students and experts, a compendium of important articles covering (1) the development of single-article reconstruction techniques, and (2) the progress in the exploration of structural basis of translation in bacteria and eukaryotes by cryo-EM and single-particle reconstruction.For novice and expert alike, a good overview of the development of tools and the ensuing discoveries spanning almost half a century has been lacking. Review articles attempting such an endeavor normally a very limited scope. The purpose of this book is to give the reader access to a selection of original articles spanning this period, from which he or she can form his or her opinion, the introductory text serving as a guide.There is no competing book. The author has made pioneering contributions both in the development of the technique, which is now on the verge of attaining atomic resolution, and to the exploration of ribosome structure and function.Selected reprints of key papers in the development of single-particle reconstruction methods, and in the research of ribosome structure and dynamics making use of these new methods. The reprints cover the period of 1969–2013.

This book is published to celebrate the International Year of Crystallography 2014, as proclaimed by the United Nations. The year has been chosen as the International Year of Crystallography since it was 100 years ago that the first Nobel Prize was awarded for crystallographic observations to Max von Laue. Just a year later, Sir William Henry Bragg and William Lawrence Bragg, father and son, won their prize for showing the possibility of determining atomic positions in crystals. This book describes the lives and works of 33 Nobel Laureates starting with Wilhelm Conrad Röntgen (1901) and ending with Brian Kobilka (2012). It also reproduces the most important works of these scientists. The book gives a historical perspective of a scientific field that is important for our understanding of the atomic organization of the world around us, from inorganic materials to complex biological molecules, such as the ribosome.This book is a timely summary of the main developments in crystallography over the last 100 years. The central publications of 33 Nobel laureates are reproduced. There is no other book providing this selection of material.

This unique volume reviews the beautiful architectures and varying mechanical actions of the set of specialized cellular proteins called molecular chaperones, which provide essential kinetic assistance to processes of protein folding and unfolding in the cell. Ranging from multisubunit ring-shaped chaperonin and Hsp100 machines that use their central cavities to bind and compartmentalize action on proteins, to machines that use other topologies of recognition — binding cellular proteins in an archway or at the surface of a "clamp" or at the surface of a globular assembly — the structures show us the ways and means the cell has devised to assist its major effectors, proteins, to reach and maintain their unique active forms, as well as, when required, to disrupt protein structure in order to remodel or degrade. Each type of chaperone is beautifully illustrated by X-ray and EM structure determinations at near- atomic level resolution and described by a leader in the study of the respective family. The beauty of what Mother Nature has devised to accomplish essential assisting actions for proteins in vivo is fully appreciable.

The current book attempts to give a glimpse of the scientific life of Michael Rossmann. The book begins with his very interesting and moving autobiography. His enormous energy must have been evident already from early childhood when he and his mother had to emigrate from Nazi-Germany to England, via The Netherlands. Starting school with a new language was a challenge that he managed well with the assistance of understanding teachers. Crystallography soon became the tool to explore new worlds, unknown to everybody. With a skill for mathematics, he realized that the transform of a molecular structure in the diffraction pattern could be used for analysis of both symmetry and structural relationships. This method, molecular replacement (MR, also the initials of his name) became one of his great successes of his career. The previous book by him in this series (Selected Papers by Michael G Rossmann with Commentaries) covers his main contributions in this area.With an interest in symmetry, viruses became obvious objects to study. Rossmann attacked these monstrously large molecular assemblies with his unfailing energy and his appetite for real challenges. The amazing variation of molecular arrangements with icosahedral symmetry is truly amazing. This book includes a selection of reports of the structures of some giant viruses. As always, knowing the structure enhances the understanding of function greatly, in the case of viruses the mechanism of infection is a key problem. Rossmann has contributed many central insights in this area.Thus, this book is of interest both as an interesting personal story but also for research into viruses that repeatedly plague all living organisms on the planet, right now in the form of the corona virus pandemic.

The book provides a synthetic and exhaustive view of how proteins have evolved their structure to accommodate a variety of metal ions in order to accomplish the most demanding chemical reactions that sustain life. This book may be the subject of a monographic course on its own or may complement bioinorganic chemistry textbooks to obtain a comprehensive view of the structural aspects of this subject. It is directed at advanced undergraduate and graduate students, researchers, instructors, and professors teaching in protein science, biochemistry, cell biology.This is the first textbook focused on 3D-structures of metalloproteins. It is also a tool for a monographic course on one or more biogeochemical cycles of metal ions. It provides a comprehensive overview of the structural chemistry of metal ions in proteins.

This book provides a glimpse into the life and work of Robert Langer, an amazing scientist, inventor and entrepreneur. Growing up in Albany, New York, Langer developed a passion for mathematics. While he was pretty good at science, he was very good at math. He went on to receive his BA in chemical engineering from Cornell University and his Doctorate of Science from the Massachusetts Institute of Technology. As a graduate student at MIT, he was involved in teaching underprivileged high school dropouts, his goal: to make math and science interesting.Langer's research laboratory at MIT is the largest biomedical engineering lab in the world. He has authored more than 1300 papers and holds more than 1080 patents. His patents have been licensed or sublicensed to more than 250 companies. A selection of 53 key papers and 50 patents are included in this book.Langer has pioneered many new technologies, including controlled release system and is regarded as the founder of tissue engineering in the field of regenerative medicine. However, his success did not come easily. He struggled in the late 1970s and early 1980s because scientists, especially established scientists, did not believe in his research. To obtain his first patent, Langer scoured existing literature and found a paper published by five famous chemists and chemical engineers that said his results were surprising and went against conventional thinking. He managed to get the patent after the five researchers confirmed that they really wrote the paper.The introductory chapter of the book gives an account of Langer's struggles as well as triumphs as he pursued research in biotechnology and tissue engineering in an effort to "make the world a better place and transform human healthcare." The book will appeal to both students and scientists.