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This volume reviews the latest development in production, stabilization and structural analysis techniques of membrane proteins. It contains 14 chapters exploring topics including the advances in heterologous expression systems, stabilization tools and structural methods that contributed to the growing number of recombinant integral membrane protein structures solved in the past few years. Each chapter was written by internationally renowned scientists in the field of membrane proteins structural characterization. Membrane proteins account for roughly 30 percent of all open reading frames in fully sequenced genomes. However, to date, atomic structures have so far been obtained for only 424 integral membrane proteins, with 100 new structures determined in the last two years. Only 10 percent of the unique integral membrane protein structures are derived from vertebrates. In general, integral membrane proteins are present in tissues at very low concentration, making production of recombinant proteins in heterologous systems suitable for large scale production a prerequisite for structural studies. Since the first atomic structures of recombinant mammalian integral membrane proteins published in 2005 (the calcium ATPase SERCA 1A and a voltage-dependent potatium channel), the structures of 37 recombinant mammalian integral membrane proteins, from which 20 belong to the G Protein Coupled Receptors family, have been solved.

Chemical structure --- Biomembranes --- Histology. Cytology --- General biochemistry --- Biology --- celmembranen --- membranen (biologie) --- protein-engineering --- biochemie --- biologie --- cytologie --- histologie --- eiwitten --- moleculaire biologie

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Molecular chaperones are a fundamental group of proteins that have been identified only relatively recently. They are key components of a protein quality machinery in the cell which insures that the folding process of any newly-synthesized polypeptide chain results in the formation of a properly folded protein and that the folded protein is maintained in an active conformation throughout its functional lifetime. Molecular chaperones have been shown to play essential roles in cell viability under both normal and stress conditions. Chaperones can also assist in the unfolding and degradation of misfolded proteins and in disaggregating preformed protein aggregates. Chaperones are also involved in other cellular functions including protein translocation across membranes, vesicle fusion events, and protein secretion. In recent years, tremendous advances have been made in our understanding of the biology, biochemistry, and biophysics of function of molecular chaperones. In addition, recent technical developments in the fields of proteomics and genomics allowed us to obtain a global view of chaperone interaction networks. Finally, there is now a growing interest in the role of molecular chaperones in diseases. This book will provide a comprehensive analysis of the structure and function of the diverse systems of molecular chaperones and their role in cell stress responses and in diseases from a global network perspective.

Chemical structure --- General biochemistry --- Biology --- Human biochemistry --- Biotechnology --- medische biochemie --- protein-engineering --- proteomics --- genomics --- biochemie --- biologie --- biotechnologie --- eiwitten --- moleculaire biologie

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This book focuses on the application of fluorescence to study motor proteins (myosins, kinesins, DNA helicases and RNA polymerases). It is intended for a large community of biochemists, biophysicists and cell biologists who study a diverse collection of motor proteins. It can be used by researchers to gain an insight into their first experiments, or by experienced researchers who are looking to expand their research to new areas. Each chapter provides valuable advice for executing the experiments, along with detailed background knowledge in order to develop own experiments.

Chemical structure --- Histology. Cytology --- General biochemistry --- Biology --- protein-engineering --- biochemie --- biologie --- cytologie --- histologie --- eiwitten --- polymeren --- moleculaire biologie

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In this brief, Vladimir Uversky discusses the paradigm-shifting phenomenon of intrinsically disordered proteins (IDPs) and hybrid proteins containing ordered domains and functional IDP regions (IDPRs). Beginning with an introduction to the concept of protein intrinsic disorder, Uversky then goes on to describe the peculiar amino acid sequences of IDPs, their structural heterogeneity, typical functions and disorder-based binding modes. In the final sections, Uversky discusses IDPs in human diseases and as potential drug targets. This volume provides a snapshot to researchers entering the field as well as providing a current overview for more experienced scientists in related areas.

Chemical structure --- General biochemistry --- Biology --- Clinical chemistry --- moleculaire structuur --- klinische chemie --- medische chemie --- biochemie --- biologie --- eiwitten --- moleculaire biologie

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This first of two volumes provides a general overview of the genetics, structure, mechanism and regulation of the Ras superfamily proteins and describes in detail the signaling pathways and processes regulated by specific members of this family. The focus of this first volume is on the Rho and Ras subfamily of small G proteins. Renowned scientists provide insights into the biochemistry of the classical and non-classical small G-protein family members, their spatio-temporal regulation, their effectors and their roles in health and disease. Together with Volume 2, this book provides a comprehensive and state-of-the-art work on small G-proteins (GTPases). It is intended for graduates and professors in biochemistry and cell biology already working on small G-proteins (small GTPases), but also offers an extremely valuable resource for those readers who are new to the field.

Chemical structure --- Histology. Cytology --- General biochemistry --- Biology --- moleculaire structuur --- protein-engineering --- biochemie --- biologie --- cytologie --- histologie --- eiwitten --- moleculaire biologie