Download or read book Structure And Action Of Molecular Chaperones Machines That Assist Protein Folding In The Cell written by Lila M Gierasch and published by World Scientific. This book was released on 2016-08-08 with total page 328 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.

Download or read book Structure and Action of Molecular Chaperones written by Lila M. Gierasch and published by World Scientific Publishing Company. This book was released on 2016 with total page 319 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.

Download or read book The Molecular Chaperones Interaction Networks in Protein Folding and Degradation written by Walid A. Houry and published by Springer. This book was released on 2014-09-01 with total page 481 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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. ​

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.

Download or read book Role of Molecular Chaperones in Structural Folding Biological Functions and Drug Interactions of Client Proteins written by Mario D. Galigniana and published by Bentham Science Publishers. This book was released on 2018-04-26 with total page 279 pages. Available in PDF, EPUB and Kindle. Book excerpt: The book provides an updated panorama of the functional relevance of molecular chaperones in the proper folding of client factors, protein-protein interactions, the regulation of key biological functions, the development of ligand-based structural complexes and the consequent pharmacological or biotechnological applications of these processes. The involvement of molecular chaperones in several processes ranging from regulation of transcription factors and protein-protein interactions in bacteria to proteostasis, signaling pathways and cancer are also addressed. The book is an essential consulting tool for researchers, working professionals in academia or industry, and students of all levels who wish to obtain the most relevant and updated information currently available about protein folding and chaperones.

Download or read book The Networking of Chaperones by Co chaperones written by Gregory Lloyd Blatch and published by Springer. This book was released on 2014-12-08 with total page 286 pages. Available in PDF, EPUB and Kindle. Book excerpt: Co-chaperones are important mediators of the outcome of chaperone assisted protein homeostasis, which is a dynamic balance between the integrated processes of protein folding, degradation and translocation. The Networking of Chaperones by Co-chaperones describes how the function of the major molecular chaperones is regulated by a cohort of diverse non-client proteins, known as co-chaperones. The second edition includes the current status of the field and descriptions of a number of novel co-chaperones that have been recently identified. This new edition has a strong focus on the role of co-chaperones in human disease and as putative drug targets. The book will be a resource for both newcomers and established researchers in the field of cell stress and chaperones, as well as those interested in cross-cutting disciplines such as cellular networks and systems biology.

Download or read book Protein Folding and Aggregation in the Presence of the Hsp70 Chaperone written by Miranda F. Mecha and published by . This book was released on 2021 with total page 0 pages. Available in PDF, EPUB and Kindle. Book excerpt: Most life on earth depends on ribosome-assisted biosynthesis and on the generation and preservation of correct protein structure. Molecular chaperones and their cochaperones act co- and post-translationally to promote de novo protein folding, overcome protein damage upon stress and even disaggregate protein aggregates. Hsp70, a ubiquitous and highly conserved 70 kDa heat shock protein, is a particularly important and well-studied chaperone. It is often referred to as a central "hub" due to its myriad of functions and its profound effect on cell viability. While the Hsp70 chaperone cycle has been well-documented in the literature, there is still much to be understood about the interplay between Hsp70 and its client-proteins, including the kinetic and thermodynamic client-protein characteristics required for interaction with Hsp70. The Hsp70 chaperone is nucleotide-dependent and derives part of its driving force for assisting protein folding from ATP hydrolysis. The Hsp70-related studies carried out to date bear an apparent inconsistency. Namely, some proteins were reported to attain their native state more slowly in the presence of the Hsp70 chaperone than under chaperone-free conditions. On the other hand, aggregation-prone proteins routinely acquire a bioactive native state faster, in the presence of Hsp70. Part of the work carried out in this thesis attempts to explain this apparent inconsistency. In addition, we explore the kinetic and thermodynamic client-protein characteristics necessary for interaction with the Hsp70 chaperone. Finally, we address the relation between protein aging and Hsp70-chaperone activity.The thesis is divided into six chapters. Chapter 1 delves into the current literature and summarizes what is known about protein folding and how the folding process is influenced by the Hsp70 chaperone cycle. This chapter further discusses the structure and function of Hsp70 and how these characteristics affect the conformation and dynamics of chaperone-bound client proteins. The chapter also provides a brief overview of the current computational approaches to predict the timecourse of Hsp70-assisted protein folding. Chapter 2 focuses on the development of CHAMPION70, a computational model able to perform Chaperone-Mediated Protein folding kinetic Simulations involving Hsp70. We then apply CHAMPION70 to four classes of client proteins with different kinetic (fast- or slow-folding) and thermodynamic (stable or unstable) stabilities in the presence of either no aggregation, weak aggregation or strong aggregation propensities. We find that, in the absence of aggregation, unstable client proteins capture (i.e., stay bound to) the Hsp70 chaperone indefinitely. This is a clear disadvantage unless Hsp70 serves as a transport machine, for these proteins. Conversely, in the presence of weak or strong aggregation propensities, it is very beneficial for client-proteins to interact with the Hsp70 chaperone system. Specifically, slow-folding and thermodynamically stable client proteins experience the greatest aggregation-prevention advantages in the presence of Hsp70, especially if the class of client proteins is strongly aggregation-prone. However, Hsp70 is unable to assist the folding of strongly aggregation-prone and thermodynamically unstable proteins. Importantly, we also predict that the E. coli Hsp70 chaperone system is unable to prevent protein aggregation over long time spans long-term (i.e., greater than ca 60 years). This result suggests that one of the consequence of protein aging is the intrinsic failure of the bacterial Hsp70 chaperone machinery. Of course E. coli bacteria double in only a few minutes and "old proteins" likely persist in the progeny (i.e., daughter cells). Yet these old proteins progressively become more and more dilute, hence less-aggregation-prone. This phenomenon may rescue bacteria from disaster. Yet one wonders whether this effect may have a more severe impact on eukaryotic Hsp70s. In summary, the CHAMPION70 simulator is a powerful tool to enable the prediction of client-protein behavior in the presence of one of the most amazing cellular machines, the Hsp70 chaperone system. Chapter 3 provides simple computational tools to discriminate folded from intrinsically disordered proteins (IDPs) under physiologically relevant conditions, solely based on protein amino-acid composition. This tool only requires knowledge on protein hydrophobicity-per-residue and net-charge-per-residue. The net-charge-non-polar (NECNOP) algorithm results in 95% accuracy, and this value increases for proteins of more than 140 residues. Chapter 4 delves into influence of the E. coli ribosome on both co- and post-translational protein folding in the absence typical molecular chaperone systems (DnaK, trigger factor) and in the presence of aggregation. In this experimental investigation, translation through the ribosome is found to promote nascent-protein solubility even in the absence of cotranslationally active molecular chaperones. This work also shows that the E. coli trigger factor and DnaK molecular chaperones increase the solubility of nascent chains emerging from the ribosomal exit tunnel and minimize co- and post-translational aggregation. Most importantly, this work shows the importance of immediately post-translational kinetic partitioning of nascent proteins between native-state and aggregates, upon release form the ribosome. This partitioning is dramatically sensitive to subtle variations in amino-acid sequence, including single-point mutations. Chapter 5 demonstrates the increased sensitivity of the NMR hyperpolarization technique known as low-concentration photochemically induced dynamic nuclear polarization (LC-photo-CIDNP). This technique is used for detection of aromatic amino acids in the presence of both a photosensitizer dye (fluorescein) and a cryogenic probe. Experiments rapidly detect the amino acids tryptophan (Trp) and tyrosine (Tyr) at unprecedented concentrations (200 nM). Detection of the model protein drkN SH3 (which bears Trp, Tyr and His) at 500 nM on a 600 MHz spectrometer via LC-Photo-CIDNP leads to a 30-fold better S/N relative to conventional 2D experiments performed at higher magnetic field (900MHz spectrometer). Spectral editing of the model protein allowed for secondary and tertiary structure analysis. In contrast to regular photo-CIDNP, LC-photo-CIDNP does not heavily depend on laser intensity, thus allowing for safer and more cost-effective experiments. Chapter 6 further develops the investigations of Chapter 5 on LC-photo-CIDNP. A major limitation of LC-photo-CIDNP is that a limited number of scans (up to ca 200) can typically be collected before sample degradation takes over. The signal-to-noise (SN) ratio becomes progressively weaker as the number of scans increases. This disadvantage strongly limits the ability to perform long-term experiments. Two reductive radical quenchers - ascorbic acid (vitamin C) and 2-mercaptoethylamine (MEA) - were employed in this study, to minimize the extent of photodamage in NMR samples. This technique both enhanced the S/N by over 100% and allowed for more transients to be acquired for amino-acid and protein samples in solution.

Download or read book Regulation of Heat Shock Protein Responses written by Alexzander A A Asea and published by Springer. This book was released on 2018-05-01 with total page 471 pages. Available in PDF, EPUB and Kindle. Book excerpt: This books provides the most up-to-date reviews on current advances in our understanding of the regulation of heat shock protein responses. Key basic scientists and clinical research laboratories from major universities, academic medical centers and pharmaceutical companies around the world have contributed chapters that review present research activity and importantly project this field into the future. For easy readability, the book is sub divided into four sections, including, Section I - HSP and Stress Responses; Section II - Chaperone Functions of HSP; Section III - HSP in Human Diseases; Section IV - Prognosis & Diagnosis of HSP. The book is a must read for researchers involved in biomedical research, drug discovery and design to improve human health.

Download or read book The Chaperonins written by Robert L. Ellis and published by Elsevier. This book was released on 1996-04-01 with total page 339 pages. Available in PDF, EPUB and Kindle. Book excerpt: The first of its kind, this volume presents the latest research findings on the chaperonins, the best studied family of a class of proteins known as molecular chaperones. These findings are changing our view of some fundamental cellular processes involving proteins, especially how proteins fold into their functional conformations. Origins of the new view of protein folding Prokaryotic chaperonins Eukaryotic chaperonins Evolution of the chaperonins Refolding of denatured proteins Organelle biosynthesis Biomedical aspects

Download or read book The Chaperonopathies written by Alberto J.L. Macario and published by Springer Science & Business Media. This book was released on 2013-04-10 with total page 126 pages. Available in PDF, EPUB and Kindle. Book excerpt: This Brief provides a concise review of chaperonopathies, i.e., diseases in which molecular chaperones play an etiologic-pathogenic role. Introductory chapters deal with the chaperoning system and chaperoning teams and networks, HSP-chaperone subpopulations, the locations and functions of chaperones, and chaperone genes in humans. Other chapters present the chaperonopathies in general, including their molecular features and mechanistic classification into by defect, excess, or mistake. Subsequent chapters discuss the chaperonopathies in more detail, focusing on their distinctive characteristics: primary or secondary; quantitative and/or qualitative; structural and hereditary or acquired; genetic polymorphisms; gene dysregulation; age-related; associated with cancer, chronic inflammatory conditions, and autoimmune diseases. The interconnections between the chaperoning and the immune systems in cancer development, chronic inflammation, autoimmunity, and ageing are outlined, which leads to a discussion on the future prospects of chaperonotherapy. The latter may consist of chaperone gene and protein replacement/supplementation in cases of deficiency and of gene or protein blocking when the chaperone actively promotes disease. The last chapter presents the extracellular chaperones and details on how the chaperone Hsp60 is secreted into the extracellular space and, thus, appears in the blood of cancer patients with potential to participate in carcinogenesis and chronic inflammation and autoimmunity. Chaperones as clinically useful biomarkers are mentioned when pertinent. Likewise, guidelines for clinical evaluation of chaperonopathies and for their histopathological and molecular identification are provided throughout. The book also provides extensive bibliography organized by chapter and topic with comments.

Download or read book Molecular Chaperones and Folding Catalysts written by Bernd Bakau and published by CRC Press. This book was released on 2003-09-02 with total page 784 pages. Available in PDF, EPUB and Kindle. Book excerpt: One of the most intriguing discoveries in molecular biology in the last decade is the existence of an evolutionary conserved and essential system, consisting of molecular chaperones and folding catalysts, which promotes the folding of the proteins in the cell. This text summarizes our current knowledge of the cellular roles, the regulation and the mechanism of action of this system. It has a broad scope, covering cell biological, genetic and biochemical aspects of protein folding in cells from bacteria to man. Particularly appropriate to researchers working in basic and applied aspects of molecular medicine, this volume should also prove useful as an up-to-date reference book and as a textbook for specialized university courses.

Download or read book Prokaryotic Chaperonins written by C. M. Santosh Kumar and published by Springer. This book was released on 2017-08-30 with total page 172 pages. Available in PDF, EPUB and Kindle. Book excerpt: This book focuses on a topical and timely aspect of prokaryotic biology - the biology of prokaryotic multiple chaperonins. Chaperonins are a class of molecular chaperones, the proteins that assist folding of other proteins in the cell. The book begins with an introductory chapter on the structural and functional aspects of chaperonins, followed by an outline on different mechanisms of their regulation. Subsequently, the book provides a comprehensive overview on how the multiple-chaperonins have embraced biological requirements in different classes of microbes, discussing their functional diversity, evolutionary paths and the latest advances in the field. It brings together leading experts from across the globe in offering a detailed account of the structural, biochemical, functional and phylogenetic characteristics of microbial chaperonins for students, researchers and teachers working in the area of microbiology/ biophysics/ parasitology – more specifically, in protein folding pathways.

Download or read book Guidebook to Molecular Chaperones and Protein Folding Catalysts written by Mary-Jane Gething and published by OUP Oxford. This book was released on 1997-11-27 with total page 586 pages. Available in PDF, EPUB and Kindle. Book excerpt: The precise shape of a protein is a crucial factor in its function. How do proteins become folded into the right conformation? Molecular chaperones and protein folding catalysts bind to developing polypeptides in the cytoplasm and ensure correct folding and transport. This Guidebook catalogues the latest information on nearly 200 of these molecules, including the important class of heat shock proteins; each entry is written by leading researchers in the field.

Download or read book Molecular Chaperones written by R.J. Ellis and published by Springer. This book was released on 2011-10-13 with total page 121 pages. Available in PDF, EPUB and Kindle. Book excerpt: Currently one of the hottest topics in biochemistry, the concept of molecular chaperones has challenged the paradigm of protein self-assembly. Key figures in many disciplines review all aspects of molecular chaperones in this volume, which arises from a Royal Society discussion meeting. Overview chapters discuss the significance of chaperones in biochemistry, molecular genetics and cell biology. Each chapter is well referenced providing access to the literature.

Download or read book Molecular Chaperones written by R.J. Ellis and published by Springer Science & Business Media. This book was released on 2012-12-06 with total page 124 pages. Available in PDF, EPUB and Kindle. Book excerpt: Currently one of the hottest topics in biochemistry, the concept of molecular chaperones has challenged the paradigm of protein self-assembly. Key figures in many disciplines review all aspects of molecular chaperones in this volume, which arises from a Royal Society discussion meeting. Overview chapters discuss the significance of chaperones in biochemistry, molecular genetics and cell biology. Each chapter is well referenced providing access to the literature.

Download or read book Abiotic Stress Response in Plants written by Narendra Tuteja and published by John Wiley & Sons. This book was released on 2016-01-08 with total page 456 pages. Available in PDF, EPUB and Kindle. Book excerpt: Understanding abiotic stress responses in plants is critical for the development of new varieties of crops, which are better adapted to harsh climate conditions. The new book by the well-known editor team Narendra Tuteja and Sarvajeet Gill provides a comprehensive overview on the molecular basis of plant responses to external stress like drought or heavy metals, to aid in the engineering of stress resistant crops. After a general introduction into the topic, the following sections deal with specific signaling pathways mediating plant stress response. The last part covers translational plant physiology, describing several examples of the development of more stress-resistant crop varieties.

Download or read book Handbook of Molecular Chaperones written by Piero Durante and published by Nova Science Publishers. This book was released on 2010 with total page 0 pages. Available in PDF, EPUB and Kindle. Book excerpt: Molecular chaperones are a ubiquitous class of proteins that play important roles in protein folding and in the protection of cells from several stresses associated with the disruption of three native dimensional structures of proteins. The most important of these proteins are the so-called heat shock proteins (HSPs), also known as stress proteins. This book examines some of the biological aspects of this intriguing family of proteins that are important for consideration of the "proteiomics of HSPs". This book also reviews current research on protein folding in the endoplasmic reticulum (ER) and the functions of ER-resident molecular chaperones in protein folding in the ER. The biochemical, structural and functional information on Redox Enzyme Maturation Proteins (REMPs) are also reviewed in detail. Furthermore, recent progress in molecular biology has provided new insights into the molecular basis of diseases and molecular targets for diagnosis and therapy of human diseases. The role of molecular biology research in molecular imaging is examined, as well as the applications of molecular imaging in diagnostics, gene therapy and drug development. Other chapters in this book explore the role of protists as promising objects for the study of adaptive mechanisms at the biochemical and the molecular level, the different trends in the evolution of molecular adaptations to adverse environmental conditions, and a review of the molecular mechanisms of bicyclol in the protection against liver damage.