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With contributions from experts in the field, this book provides a comprehensive overview of the oxidative folding of cysteine-rich peptides.
The formation of disulphide bonds is probably the most influential modification of proteins. These bonds are unique among post-translational modifications of proteins as they can covalently link cysteine residues far apart in the primary sequence of a protein. This has the potential to convey stability to otherwise marginally stable structures of proteins. However, the reactivity of cysteines comes at a price: the potential to form incorrect disulphide bonds, interfere with folding, or even cause aggregation. An elaborate set of cellular machinery exists to catalyze and guide this process: facilitating bond formation, inhibiting unwanted pairings and scrutinizing the outcomes. Only in recent years has it become clear how intimately connected this cellular machinery is with protein folding helpers, organellar redox balance and cellular homeostasis as a whole. This book comprehensively covers the basic principles of disulphide bond formation in proteins and describes the enzymes involved in the correct oxidative folding of cysteine-containing proteins. The biotechnological and pharmaceutical relevance of proteins, their variants and synthetic replicates is continuously increasing. Consequently this book is an invaluable resource for protein chemists involved in realted research and production.
This book aims to cover the knowledge of protein folding accumulated from studies of disulfide-containing proteins, including methodologies, folding pathways, and folding mechanism of numerous extensively characterized disulfide proteins. Folding of Disulfide Proteins will be valuable supplementary reading for general biochemistry, biophysics, molecular biology, and cellular biology courses for graduate and undergraduate students. This book can also be used for specialized graduate-level biochemistry, biophysics, and molecular biology courses dedicated to protein folding as well as related biological problems and diseases. Will also be of interest to everybody interested in problems related to protein folding, and anyone who is interested in understanding the mechanism of protein misfolding and protein misfolding-related diseases.
This is the last of five books in the Amino Acids, Peptidesand Proteins in Organic Synthesis series. Closing a gap in the literature, this is the only series tocover this important topic in organic and biochemistry. Drawingupon the combined expertise of the international "who's who" inamino acid research, these volumes represent a real benchmark foramino acid chemistry, providing a comprehensive discussion of theoccurrence, uses and applications of amino acids and, by extension,their polymeric forms, peptides and proteins. The practical value of each volume is heightened by theinclusion of experimental procedures. The 5 volumes cover the following topics: Volume 1: Origins and Synthesis of Amino Acids Volume 2: Modified Amino Acids, Organocatalysis and Enzymes Volume 3: Building Blocks, Catalysis and Coupling Chemistry Volume 4: Protection Reactions, Medicinal Chemistry,Combinatorial Synthesis Volume 5: Analysis and Function of Amino Acids and Peptides Volume 5 of this series presents a wealth of methods to analyzeamino acids and peptides. Classical approaches are described, suchas X-ray analysis, chromatographic methods, NMR, AFM, massspectrometry and 2D-gel electrophoresis, as well as newerapproaches, including Surface Plasmon Resonance and arraytechnologies. Originally planned as a six volume series, Amino Acids,Peptides and Proteins in Organic Chemistry now completes withfive volumes but remains comprehensive in both scope andcoverage. ahref="http://eu.wiley.com/WileyCDA/WileyTitle/productCd-3527335463.html"Furtherinformation about the 5 Volume Set and purchasing details can beviewed here./a
Explains the role of reactive intermediates in biological systems as well as in environmental remediation With its clear and systematic approach, this book examined the broad range of reactive intermediate that can be generated in biological environments, detailing the fundamental properties of each reactive intermediate. Readers gain a contemporary understanding of how these intermediates react with different compounds, with an emphasis on amino acids, peptides, and proteins. The author not only sets forth the basic chemistry and nature of reactive intermediates, he also demonstrates how the properties of the intermediates presented in the book compare with each other. Oxidation of Amino Acids, Peptides, and Proteins begins with a discussion of radical and non-radical reactive species as well as an exploration of the significance of reactive species in the atmosphere, disinfection processes, and environmental remediation. Next, the book covers such topics as: Thermodynamics of amino acids and reactive species and the effect of metal-ligand binding in oxidation chemistry Kinetics and mechanisms of reactive halogen, oxygen, nitrogen, carbon, sulfur and phosphate species as well as reactive high-valent Cr, Mn, and Fe species Reactivity of the species with molecules of biological and environmental importance Generation of reactive species in the laboratory for kinetics studies Oxidation of amino acids, peptides, and proteins by permanganate, ferryl, and ferrate species Application of reactive species in purifying water and treating wastewater With this book as their guide, readers will be able to assess the overall effects of reactive intermediates in biological environments. Moreover, they’ll learn how to apply this knowledge for successful water purification and wastewater treatment.
This volume of Advances in Protein Chemistry provides a broad, yet deep look at the cellular components that assist protein folding in the cell. This area of research is relatively new--10 years ago these components were barely recognized, so this book is a particularly timely compilation of current information. Topics covered include a review of the structure and mechanism of the major chaperone components, prion formation in yeast, and the use of microarrays in studying stress response. Outlines preceding each chapter allow the reader to quickly access the subjects of greatest interest. The information presented in this book should appeal to biochemists, cell biologists, and structural biologists.
Oxidative protein folding describes the process by which disulfide bonds are inserted into proteins as they fold into their native structure. This involves two distinct phases, an oxidation phase where these covalent linkages are first introduced, and an isomerization phase in which incorrectly placed disulfides are shuffled leading to the native pairings. In eukaryotes, disulfide bond formation can be catalyzed by a number of flavin-dependent sulfhydryl oxidases. This dissertation work investigates how a particular flavin-dependent sulfhydryl oxidase, Quiescin-sulfhydryl oxidase (QSOX), cooperates with protein disulfide isomerase (PDI) to generate native pairings in two unfolded reduced proteins: ribonuclease A (RNase A, four disulfide bonds and 105 disulfide isomers of the fully oxidized protein) and avian riboflavin binding protein (RfBP, nine disulfide bonds and more than 34 million corresponding disulfide pairings). This QSOX/PDI in vitro folding system involves no functional interaction between the two enzymatic components; QSOX inserts disulfide bonds into protein substrates while PDI isomerizes the misplaced pairs to the native ones. Rapid refolding does not require glutathione or glutathione-based redox buffers. Refolding of RfBP is followed continuously by monitoring spectral changes experienced by the ligand, riboflavin, upon binding to the apoprotein. Efficient refolding of this protein only occurs with a large molar excess of reduced PDI over the folding client protein. These conditions likely mirror the environment of the endoplasmic reticulum lumen where small concentrations of nascent proteins are exposed to nearly mM levels of PDI. Subsequent studies performed in the absence of QSOX or redox buffers, explore the effectiveness of mixtures of oxidized and reduced PDI in refolding RfBP. Here, the fastest refolding of RfBP occurs with excess reduced PDI and just enough oxidized PDI to generate nine disulfides in the protein. The implications of these in vitro experiments for understanding oxidative folding processes in vivo are discussed. Although unfolded proteins have been proven to be excellent substrates of QSOX, a recent proposal suggests that it can also function in the generation of inter-domain and inter-protein disulfide bridges, where the substrates are already substantially or completely folded. This suggestion has been tested using wild type and mutant Escherichia coli thioredoxin as a model substrate. These folded substrates are, by comparison, poorly oxidized by QSOX which is consistent with the expected stringent steric requirements for efficient thiol/disulfide exchange reactions.
PROVIDES STRATEGIES AND CONCEPTS FOR UNDERSTANDING CHEMICAL PROTEOMICS, AND ANALYZING PROTEIN FUNCTIONS, MODIFICATIONS, AND INTERACTIONS—EMPHASIZING MASS SPECTROMETRY THROUGHOUT Covering mass spectrometry for chemical proteomics, this book helps readers understand analytical strategies behind protein functions, their modifications and interactions, and applications in drug discovery. It provides a basic overview and presents concepts in chemical proteomics through three angles: Strategies, Technical Advances, and Applications. Chapters cover those many technical advances and applications in drug discovery, from target identification to validation and potential treatments. The first section of Mass Spectrometry-Based Chemical Proteomics starts by reviewing basic methods and recent advances in mass spectrometry for proteomics, including shotgun proteomics, quantitative proteomics, and data analyses. The next section covers a variety of techniques and strategies coupling chemical probes to MS-based proteomics to provide functional insights into the proteome. In the last section, it focuses on using chemical strategies to study protein post-translational modifications and high-order structures. Summarizes chemical proteomics, up-to-date concepts, analysis, and target validation Covers fundamentals and strategies, including the profiling of enzyme activities and protein-drug interactions Explains technical advances in the field and describes on shotgun proteomics, quantitative proteomics, and corresponding methods of software and database usage for proteomics Includes a wide variety of applications in drug discovery, from kinase inhibitors and intracellular drug targets to the chemoproteomics analysis of natural products Addresses an important tool in small molecule drug discovery, appealing to both academia and the pharmaceutical industry Mass Spectrometry-Based Chemical Proteomics is an excellent source of information for readers in both academia and industry in a variety of fields, including pharmaceutical sciences, drug discovery, molecular biology, bioinformatics, and analytical sciences.