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Oxidative Folding Of Peptides And Proteins
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Book Synopsis Oxidative Folding of Peptides and Proteins by : Luis Moroder
Download or read book Oxidative Folding of Peptides and Proteins written by Luis Moroder and published by Royal Society of Chemistry. This book was released on 2009 with total page 453 pages. Available in PDF, EPUB and Kindle. Book excerpt: With contributions from experts in the field, this book provides a comprehensive overview of the oxidative folding of cysteine-rich peptides.
Book Synopsis Oxidative Folding of Proteins by : Matthias J Feige
Download or read book Oxidative Folding of Proteins written by Matthias J Feige and published by Royal Society of Chemistry. This book was released on 2018-07-30 with total page 450 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.
Book Synopsis Folding of Disulfide Proteins by : Rowen J. Y. Chang
Download or read book Folding of Disulfide Proteins written by Rowen J. Y. Chang and published by Springer Science & Business Media. This book was released on 2011-08-12 with total page 290 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.
Download or read book Protein Folding in the Cell written by and published by Elsevier. This book was released on 2002-02-20 with total page 516 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.
Book Synopsis Oxidative Protein Folding in Vitro by : Pumtiwitt C. Rancy
Download or read book Oxidative Protein Folding in Vitro written by Pumtiwitt C. Rancy and published by . This book was released on 2010 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.
Book Synopsis Biochemical Basis of Oxidative Protein Folding in the Endoplasmic Reticulum by : Benjamin Peng-Chu Tu
Download or read book Biochemical Basis of Oxidative Protein Folding in the Endoplasmic Reticulum written by Benjamin Peng-Chu Tu and published by . This book was released on 2003 with total page 246 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Oxidation of Amino Acids, Peptides, and Proteins by : Virender K. Sharma
Download or read book Oxidation of Amino Acids, Peptides, and Proteins written by Virender K. Sharma and published by John Wiley & Sons. This book was released on 2012-11-06 with total page 349 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.
Book Synopsis Impact of an Easily Reducible Disulfide Bond on the Oxidative Folding Rate of Multi-disulfide-containing Proteins by : Howard J. Leung
Download or read book Impact of an Easily Reducible Disulfide Bond on the Oxidative Folding Rate of Multi-disulfide-containing Proteins written by Howard J. Leung and published by . This book was released on 2005 with total page 56 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis From Peptides to Proteins by : Robert Aron Broom
Download or read book From Peptides to Proteins written by Robert Aron Broom and published by . This book was released on 2010 with total page 88 pages. Available in PDF, EPUB and Kindle. Book excerpt: Understanding the origin of protein folds, and the mechanism by which evolution has generated them, is a critically important step on a path towards rational protein design. Modifying existing proteins and designing our own novel folds and functions is a lofty but achievable goal, for which there are many foreseeable rewards. It is believed that modern proteins may have arisen from a primordial set of peptide precursors, which were initially only pseudo-stable or stable only as complexes with RNA, and later were able to self-assemble into multimeric complexes that resembled modern folds. In order to experimentally examine the feasibility of this theory, an attempt was made at reconstructing the evolutionary path of a beta-trefoil. The beta-trefoil is a naturally abundant fold or superfold, possessing pseudo-threefold symmetry, and usually having a sugar-binding function. It has been proposed that such a fold could arise from the triplication of just one small peptide on the order of 40-50 amino acids in length. The evolutionary path of a ricin, a family within the beta-trefoils known to possess a carbohydrate binding function was the chosen template for evolutionary modelling. It was desirable to have a known function associated with this design, such that it would be possible to determine if not only the fold, but also the function, could be reconstructed. A small peptide of 47 amino acids was designed and expressed. This peptide not only trimerized as expected, but possessed the carbohydrate binding function it was predicted to have. In an evolutionary model of the early protein world, the gene for this peptide would undergo duplication and later, triplication, eventually resulting in a completely symmetrical beta-trefoil, which would represent the first modern beta-trefoil fold. Such a completely symmetrical protein was also designed and expressed by triplicating the gene for the aforementioned small peptide. This hypothetical first modern beta-trefoil is: well folded, stable, soluble, and appears to adopt a beta-trefoil fold. Together these results demonstrate that an evolutionary model of early life: that proteins first existed as self-assembling modular peptides, and subsequent to gene duplications or fusions, as what we now recognize as modern folds, is experimentally consistent and not only generates stable structures, but those with function, which of course is a prime requisite of evolution. Moreover the results show that it may be possible to use this modular nature of protein folding to design our own proteins and predict the structure of others.
Book Synopsis Protein Folding, Misfolding and Aggregation by : Victor Muñoz
Download or read book Protein Folding, Misfolding and Aggregation written by Victor Muñoz and published by Royal Society of Chemistry. This book was released on 2008 with total page 290 pages. Available in PDF, EPUB and Kindle. Book excerpt: Protein folding and aggregation is the process by which newly synthesized proteins fold into the specific three-dimensional structures defining their biologically active states. It has always been a major focus of research in biochemistry and has often been seen as the unsolved second part of the genetic code. In the last 10 years we have witnessed a quantum leap in the research in this exciting area. Computational methods have improved to the extent of making possible to simulate the complete folding process of small proteins and the early stages of protein aggregation. Experimental methods h.
Book Synopsis Studies on Oxidative Protein Folding and the Development of Genetically Encoded Probes for Analyte Specific Ratiometric Imaging by : Devin A. Hudson
Download or read book Studies on Oxidative Protein Folding and the Development of Genetically Encoded Probes for Analyte Specific Ratiometric Imaging written by Devin A. Hudson and published by . This book was released on 2018 with total page 144 pages. Available in PDF, EPUB and Kindle. Book excerpt: Disulfide bond formation in vivo is linked to many essential intracellular processes; protein regulation and signaling, chemical transformations, and oxidative protein folding. Oxidative protein folding is an enzyme catalyzed process which is controlled by dedicated protein thiol oxidoreductases. In this work the oxidative protein folding within the mammalian endoplasmic reticulum (ER) is examined from an enzymological perspective. Evidence for the rapid reduction of PDI by reduced glutathione is presented in the context of PDI-first pathways. Next, strategies and challenges for the determination of the concentrations of reduced and oxidized glutathione and of the ratios of PDIred:PDIox is discussed. After a discussion of the use of natively encoded fluorescent probes to report the glutathione redox poise of the ER, a complementary strategy to discontinuously survey the redox state of as many redox-active disulfides as can be identified by ratiometric LC–MS–MS methods in order to better understand redox linked species. Next, we investigate the specificity of the human Mia40/lfALR system towards non-cognate unfolded protein substrates to assess whether the efficient introduction of disulfides requires a particular amino acid sequence context or the presence of an IMS targeting signal. Mia40 is found to be effective oxidant of non-cognate substrates, but is an ineffective protein disulfide isomerase when its ability to restore enzymatic activity from scrambled RNase is compared to that of protein disulfide isomerase. Mia40’s ability to bind amphipathic peptides tested by the insulin reductase assay. The consequences of these studies, mitochondrial oxidative protein folding, and the transit of polypeptides is discussed. Finally, the development of disulfide linked genetically encoded fluorescent probes for analyte-specific imaging are demonstrated. Current classes of intracellular probes depend on the selection of binding domains that either undergo conformational changes on analyte binding or can be linked to thiol redox chemistry. Here, novel probes were designed by fusing a flavoenzyme, whose fluorescence is quenched on reduction by the analyte of interest, with a GFP domain to allow for rapid and specific ratiometric sensing. Two flavoproteins, Escherichia coli thioredoxin reductase and Saccharomyces cerevisiae lipoamide hydrogenase, were successfully developed into thioredoxin and NAD+/NADH specific probes respectively and their performance was evaluated in vitro and in vivo. These genetically encoded fluorescent constructs represent a modular approach to intracellular probe design that should extend the range of metabolites that can be quantitated in living cells.
Book Synopsis Amino Acids, Peptides and Proteins in Organic Chemistry, Analysis and Function of Amino Acids and Peptides by :
Download or read book Amino Acids, Peptides and Proteins in Organic Chemistry, Analysis and Function of Amino Acids and Peptides written by and published by John Wiley & Sons. This book was released on 2013-02-13 with total page 508 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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
Book Synopsis The Role of Protein Disulfide Isomerase (PDI) in Oxidative Folding by : Veronica Gonzalez
Download or read book The Role of Protein Disulfide Isomerase (PDI) in Oxidative Folding written by Veronica Gonzalez and published by . This book was released on 2008 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Mass Spectrometry-Based Chemical Proteomics by : W. Andy Tao
Download or read book Mass Spectrometry-Based Chemical Proteomics written by W. Andy Tao and published by John Wiley & Sons. This book was released on 2019-07-10 with total page 448 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.
Book Synopsis Protein Folding by : Lila M. Gierasch
Download or read book Protein Folding written by Lila M. Gierasch and published by . This book was released on 1990 with total page 360 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Amino Acids, Peptides and Proteins by : Etelka Farkas
Download or read book Amino Acids, Peptides and Proteins written by Etelka Farkas and published by Royal Society of Chemistry. This book was released on 2013-11-12 with total page 271 pages. Available in PDF, EPUB and Kindle. Book excerpt: Amino Acids, Peptides and Proteins comprises a comprehensive review of significant developments at this biology/chemistry interface. Each volume of this Specialist Periodical Report opens with an overview of amino acids and their applications. In keeping with the preceeding volumes in the series, this volume presents contributions from across the globe addressing the hot topics in the field. Disulfide-containing peptides and proteins are investigated by NMR, and mass spectrometry is used to determine inter-peptide distant constraints. Further chapters review the latest literature on antimicrbial peptides, modifications by Cytochrome P450 and the relaxin-family neuropeptides. Self-assembly and the moleculatr recognition of designed peptides are also discussed, and the latest in peptide and protein-based pharmaceuticals are reviewed. Volume editor Max Ryadnov also contributes a chapter on biofunctional peptide design. As the published literature in the field continues to grow, researchers in academia and industry will find this comprehensive review of the current research and thought an essential, first-stop reference.
Book Synopsis Oxidative Folding of Proteins by : Matthias J Feige
Download or read book Oxidative Folding of Proteins written by Matthias J Feige and published by Royal Society of Chemistry. This book was released on 2018-07-27 with total page 450 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.
