Protein Refolding Using Molecular Assistants
| Author | : Peter Eric Hanson |
| Publisher | : |
| Total Pages | : 526 |
| Release | : 1997 |
| Genre | : |
| ISBN | : |
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The Molecular Chaperones Interaction Networks in Protein Folding and Degradation
| Author | : Walid A. Houry |
| Publisher | : Springer |
| Total Pages | : 481 |
| Release | : 2014-09-01 |
| Genre | : Science |
| ISBN | : 1493911309 |
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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.
Structure And Action Of Molecular Chaperones: Machines That Assist Protein Folding In The Cell
| Author | : Lila M Gierasch |
| Publisher | : World Scientific |
| Total Pages | : 328 |
| Release | : 2016-08-08 |
| Genre | : Science |
| ISBN | : 9814749346 |
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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.
Protein Folding
| Author | : Grace E. Orellana |
| Publisher | : American Chemical Society |
| Total Pages | : 170 |
| Release | : 2024-05-08 |
| Genre | : Science |
| ISBN | : 0841296383 |
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Life as we know it would not exist if proteins did not fold into functional three-dimensional structures, where α-helices, loops, and β-sheets act together to form active sites that drive a myriad of biochemical reactions in the cell. The failure of this process is linked to the pathology of various diseases, such as neurodegenerative disorders like Alzheimer’s, genetic conditions (like cystic fibrosis), and cancer. It is no wonder that close to $2 billion in worldwide research funding has been devoted over the last five years (2019–2025) to helping scientists understand the molecular details of protein folding, how it can fail in ways that promote disease in humans, and clinical paths to treat or prevent diseases linked to protein misfolding. This primer is prerequisite reading to the literature on this important topic for readers new to the field. Chapter one provides exposure to the three-dimensional structure of proteins; readers will learn how to identify secondary structures, protein motifs, and domains involved in biological function. Chapter two introduces methodologies to determine the three-dimensional structure of proteins; readers will learn modern techniques to determine the secondary structure composition and the orientation of atoms in three-dimensional space. By providing exposure to how the physical environment (i.e., chemical denaturants, pH, pressure, and temperature) controls protein denaturation, readers will learn how such information can be used to study the biophysical characteristics of proteins through various probes and methodologies.
Structure and Action of Molecular Chaperones
| Author | : Lila M. Gierasch |
| Publisher | : World Scientific Publishing Company |
| Total Pages | : 319 |
| Release | : 2016 |
| Genre | : Molecular chaperones |
| ISBN | : 9789814749329 |
Download Structure and Action of Molecular Chaperones Book in PDF, ePub and Kindle
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.
Protein Refolding Via Immobilisation on Crystal Surfaces
| Author | : Katrina Ann Davidson |
| Publisher | : |
| Total Pages | : |
| Release | : 2008 |
| Genre | : |
| ISBN | : |
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Is it possible to find an easy, generic method for protein refolding? The preparation of functionally active protein molecules from the unfolded state can be a difficult task. Although there are many well-established techniques for protein refolding, such as dilution, dialysis, chromatography and others, in many instances these methods can be time consuming and inefficient. A rapid, inexpensive and simple method for protein folding is a much sought after technique. Proteins in the unfolded state (either inclusion bodies or unfolded by chemical or physical means) are generally solubilised in solutions containing urea or guanidine hydrochloride. The removal of these molecules from the protein environment is commonly utilised as a method for triggering refolding. A new method for the refolding of biomolecular species has been developed via the formation of Protein Coated Micro-crystals (PCMC). The formation of PCMC is a recently developed method for the immobilisation protein upon the surface of a watersoluble excipient (salt, amino acid or sugar) via a co-precipitation reaction in a water miscible organic solvent. These proteins can then be used as immobilised biocatalysts in both the aqueous and organic phase. In the immobilisation of unfolded, solubilised protein, the solubilising agents (e.g. urea or guanidine hydrochloride) are removed from the protein environment as they are soluble in the organic phase. The removal of these molecules initiates protein folding during the coprecipitation process. In the course of this project, a number of proteins were studied in order to observe their behaviour in this immobilisation and simultaneous folding process. Lysozyme was utilised as it is an enzyme which is relatively simple to refold from the chemically unfolded state by conventional methods such as dilution. Upon immobilisation of lysozyme from the chemically unfolded state, up to 92% of the activity of the native protein was regained. The enzyme lipase, which is notoriously difficult to fold, was also used to determine the efficiency of this method under more challenging conditions. Lipase immobilised from the chemically unfolded state was seen to regain up to 36 % of the activity of the native protein.
Protein Refolding
| Author | : George Georgiou |
| Publisher | : |
| Total Pages | : 248 |
| Release | : 1991 |
| Genre | : SCIENCE |
| ISBN | : |
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the refolding process is often the critical bottleneck in the production of high-value proteins, and recently acquired insights have yet to be translated into technological advantages. These proceedings bridge the gap between fundamental and applied studies, addressing such issues as in vivo protein folding, protein aggregation and inclusion body formation, elucidation of the folding pathway, characterization of folding intermediates, and practical considerations in protein renaturation. The symposium was part of the 199th ACS National Meeting, Boston, April 1990. Annotation copyrighted by Book News, Inc., Portland, OR
Molecular Biology of Protein Folding, Part B
| Author | : P. Michael Conn |
| Publisher | : Academic Press |
| Total Pages | : 301 |
| Release | : 2009-01-09 |
| Genre | : Science |
| ISBN | : 0080923399 |
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Nucleic acids are the fundamental building blocks of DNA and RNA and are found in virtually every living cell. Molecular biology is a branch of science that studies the physicochemical properties of molecules in a cell, including nucleic acids, proteins, and enzymes. Increased understanding of nucleic acids and their role in molecular biology will further many of the biological sciences including genetics, biochemistry, and cell biology. Progress in Nucleic Acid Research and Molecular Biology is intended to bring to light the most recent advances in these overlapping disciplines with a timely compilation of reviews comprising each volume. Follow the new editor-in-chief, P. Michael Conn, as he introduces this second thematic volume in the series – an in-depth aid to researchers who are looking for the best techniques and tools for understanding the complexities of protein folding Understand the advantages of protein folding over other therapeutic approaches and see how protein folding plays a critical role in the development of diseases such as Alzheimer’s and diabetes Decipher the rules of protein folding through compelling and timely reviews combined with chapters written by international authors in engineering, biochemistry, physics and computer science
Protein Purification
| Author | : Jan-Christer Janson |
| Publisher | : John Wiley & Sons |
| Total Pages | : 542 |
| Release | : 2012-01-03 |
| Genre | : Science |
| ISBN | : 1118002199 |
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The authoritative guide on protein purification—now completely updated and revised Since the Second Edition of Protein Purification was published in 1998, the sequencing of the human genome and other developments in bioscience have dramatically changed the landscape of protein research. This new edition addresses these developments, featuring a wealth of new topics and several chapters rewritten from scratch. Leading experts in the field cover all major biochemical separation methods for proteins in use today, providing professionals in biochemistry, organic chemistry, and analytical chemistry with quick access to the latest techniques. Entirely new or thoroughly revised content includes: High-resolution reversed-phase liquid chromatography Electrophoresis in gels Conventional isoelectric focusing in gel slabs and capillaries and immobilized pH gradients Affinity ligands from chemical and biological combinatorial libraries Membrane separations Refolding of inclusion body proteins from E. coli Purification of PEGylated proteins High throughput screening techniques in protein purification The history of protein chromatography
Mechanism of Substrate Protein Remodeling by Molecular Chaperones
| Author | : Pooja Shrestha |
| Publisher | : |
| Total Pages | : 110 |
| Release | : 2013 |
| Genre | : |
| ISBN | : |
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Protein quality control regulates the natural load of proteins by providing folding assistance or degradation mechanism to prevent misfolding or aggregation. It is maintained by the complex regulatory network of molecular chaperons. The study of such fundamental biological system helps in designing different biological applications like targeted therapeutic treatments. The goal of this work is to elucidate protein quality control mechanisms associated with chaperonin folding assistance and protein degradation. Chaperonins are large double ring assemblies that assist folding of substrate proteins (SPs) under non-permissive conditions. Spectacular ATP driven conformational changes take place within each chaperonin ring. Distinct allosteric mechanisms have been described for the two chaperonin classes. Bacterial (group I) chaperonins, such as GroEL undergo concerted subunit motions within each ring, while archaeal and eukaryotic chaperonins (group II) undergo sequential subunit motions. In the protein degradation pathway, nanomachines such as ClpP cleave the unwanted protein. Here we study four aspects regarding this problem: (1) Allosteric mechanisms of group II chaperonin, (2) Kinetics of multi-domain protein folding confined to cylindrical nanopores (3). Structural and bioinformatics analyses to understand substrate recognition mechanisms in group II chaperonin and (4) Allosteric mechanisms of ClpP.
