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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.
Molecular machines are complex biomolecules (protein, DNA, RNA and carbohydrates that consume energy in order to perform specific functions. To understand how these systems perform their functions, it is necessary to have detailed knowledge of the conformational states of these molecular machines, as well as the reaction pathways connecting them. Many of these conformational transitions take place on a timescale that is far beyond what is attainable with current molecular dynamics simulations on large and complex systems. On the other hand, experimental methods are often unable to detect the short-lived transient features occurring during such conformational transitions. Thus, breaking new g...
This book contains aseries of review papers related to the lectures given at the Third Course on Bioelectrochemistry held at Erice in November 1988, in the framework of the International School of Biophysics. The topics covered by this course, "Charge Separation Across Biomembranes, " deal with the electrochemical aspects of some basic phenomena in biological systems, such as transport of ions, ATP synthesis, formation and maintenance of ionic and protonic gradients. In the first part of the course some preliminary lectures introduce the students to the most basic phenomena and technical aspects of membrane bioelectrochemistry. The remaining part of the course is devoted to the description o...
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Knud Nierhaus, who has studied the ribosome for more than 30 years, has assembled here the combined efforts of several scientific disciplines into a uniform picture of the largest enzyme complex found in living cells, finally resolving many decades-old questions in molecular biology. In so doing he considers virtually all aspects of ribosome structure and function -- from the molecular mechanism of different ribosomal ribozyme activities to their selective inhibition by antibiotics, from assembly of the core particle to the regulation of ribosome component synthesis. The result is a premier resource for anyone with an interest in ribosomal protein synthesis, whether in the context of molecular biology, biotechnology, pharmacology or molecular medicine.
This book provides essential information on improving protein folding/stability, which is a result of the balance between the intra-molecular interactions of protein functional groups and their interactions with the solvent environment. The protein folding solvent environment mainly consists of salts, small molecule compounds, metabolites, molecular chaperones and other chemical species. Therefore, subtle change in the composition of the environment will alter the protein folding process. The importance of the solvent environment in protein folding is precisely due to the fact that various disease-causing proteopathies can be reversed by manipulating the solvent environment of the malfolded ...
Type I chaperonins are key players in maintaining the proteome of bacteria and organelles of bacterial origin. They are well known for their crucial role in mediating protein folding. For almost three decades, the molecular mechanism of chaperonin function has been the subject of intensive research. Still, surprising new mechanistic discoveries are constantly reported. It seems that we are far from having a full understanding of the chaperonin mode of action. Chaperonins are not simply protein folding machines. They also perform diverse extramitochondrial tasks, mainly related to inflammatory and signal transduction processes. This eBook constitutes ten articles highlighting the latest developments related to the divers functions of Type I chaperonins. As its title, mechanism and beyond, the collection starts with mechanistic view, continues with extracellular functions and ends with biotechnological applications of Type I chaperonins.
This new edition describes the role of heat shock proteins in the life cycle of malaria parasites, particularly in the context of intracellular parasite stages. Thoroughly revised, this work provides a general introduction to the structural and functional features of heat shock proteins with a special focus on their role as molecular chaperones in ensuring protein quality control. The emphasis is on the heat shock protein families from Plasmodium falciparum, and their role in proteostasis and the development of malaria pathology. Moreover, the authors explore the latest prospects of targeting heat shock proteins in antimalarial drug discovery either directly or in combination therapies. Read...
Leland H. Hartwell Director, Fred Hutchinson Cancer Research Center, Nobel Laureate for Medicine, 2001 Yeast has proved to be the most useful single-celled organism for studying the fundamental aspects of cell biology. Resources are now available for yeast that greatly simplify and empower new investigations, like the presence of strains with each gene deleted, each protein tagged and databases on protein–protein interactions, gene regulation, and subcellular protein location. A powerful combination of genetics, cell biology, and biochemistry employed by thousands of yeast researchers has unraveled the complexities of numerous cellular processes from mitosis to secretion and even uncovered...
This book aims to provide a comprehensive examination of the field of molecular chaperone inhibition and its application to pharmaceutical research. With several small molecule inhibitors in oncology clinical development, there is clearly intense interest in the chaperones as a molecular target. Filling a significant gap in the market by providing a detailed comparison of discovery programs across the industry, this text will find broad interest among researchers in the field of molecular chaperone pharmaceutical research, oncology research, and medicinal chemistry. Arranged into three main sections the book covers structure and function, small molecule inhibitors and concludes with a section discussing clinical perspectives. With specific chapters covering the discovery of key molecules such as, BIIB028, STA-9090, Serenex Hsp90 inhibitor, NVP-AUY922 and NVP-HSP990, this comprehensive text will be an essential treatise for researchers working in academia and industry.