Protein Folding Misfolding And Aggregation

Author : Victor Muñoz
Publisher : Royal Society of Chemistry
Page : 290 pages
File Size : 49,5 Mb
Release : 2008
Category : Science
ISBN : 9780854042579

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Protein Folding, Misfolding and Aggregation by Victor Muñoz Pdf

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.

Author : Regina Murphy,Amos Tsai
Publisher : Springer Science & Business Media
Page : 354 pages
File Size : 42,5 Mb
Release : 2007-10-12
Category : Science
ISBN : 9780387360638

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Misbehaving Proteins by Regina Murphy,Amos Tsai Pdf

This text provides an up-to-date collection of theoretical and experimental studies into protein folding, misfolding, aggregation, and stability. Additionally, issues faced during the development of protein products are illustrated. It contains an introductory chapter for readers new to the protein folding field. The book provides a thorough and clear discussion of computational approaches to understanding and modeling protein aggregation.

Author : Heinz Fabian,Dieter Naumann
Publisher : Springer Science & Business Media
Page : 244 pages
File Size : 46,5 Mb
Release : 2011-09-18
Category : Science
ISBN : 9783642222306

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Protein Folding and Misfolding by Heinz Fabian,Dieter Naumann Pdf

Infrared spectroscopy is a new and innovative technology to study protein folding/misfolding events in the broad arsenal of techniques conventionally used in this field. The progress in understanding protein folding and misfolding is primarily due to the development of biophysical methods which permit to probe conformational changes with high kinetic and structural resolution. The most commonly used approaches rely on rapid mixing methods to initiate the folding event via a sudden change in solvent conditions. Traditionally, techniques such as fluorescence, circular dichroism or visible absorption are applied to probe the process. In contrast to these techniques, infrared spectroscopy came into play only very recently, and the progress made in this field up to date which now permits to probe folding events over the time scale from picoseconds to minutes has not yet been discussed in a book. The aim of this book is to provide an overview of the developments as seen by some of the main contributors to the field. The chapters are not intended to give exhaustive reviews of the literature but, instead to illustrate examples demonstrating the sort of information, which infrared techniques can provide and how this information can be extracted from the experimental data. By discussing the strengths and limitations of the infrared approaches for the investigation of folding and misfolding mechanisms this book helps the reader to evaluate whether a particular system is appropriate for studies by infrared spectroscopy and which specific advantages the techniques offer to solve specific problems.

Author : Marina Ramirez-Alvarado,Jeffery W. Kelly,Christopher M. Dobson
Publisher : John Wiley & Sons
Page : 1311 pages
File Size : 46,6 Mb
Release : 2010-12-01
Category : Science
ISBN : 9781118031810

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Protein Misfolding Diseases by Marina Ramirez-Alvarado,Jeffery W. Kelly,Christopher M. Dobson Pdf

An increasingly aging population will add to the number of individuals suffering from amyloid. Protein Misfolding Diseases provides a systematic overview of the current and emerging therapies for these types of protein misfolding diseases, including Alzheimer's, Parkinson's, and Mad Cow. The book emphasizes therapeutics in an amyloid disease context to help students, faculty, scientific researchers, and doctors working with protein misfolding diseases bridge the gap between basic science and pharmaceutical applications to protein misfolding disease.

Author : Vladimir N. Uversky,Anthony Fink
Publisher : Springer Science & Business Media
Page : 419 pages
File Size : 54,6 Mb
Release : 2007-11-24
Category : Science
ISBN : 9780387259192

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Protein Misfolding, Aggregation and Conformational Diseases by Vladimir N. Uversky,Anthony Fink Pdf

Research indicates that most neurodegenerative diseases, systemic amyloidoses and many others, arise from the misfolding and aggregation of an underlying protein. This is the first book to discuss significant achievements in protein structure-function relationships in biochemistry, molecular biology and molecular medicine. The authors summarize recent progress in the understanding of the relationships between protein misfolding, aggregation and development of protein deposition disorders.

Author : Robert D. E. Sewell
Publisher : CRC Press
Page : 592 pages
File Size : 51,6 Mb
Release : 2007-12-03
Category : Science
ISBN : 1420007149

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Protein Misfolding in Neurodegenerative Diseases by Robert D. E. Sewell Pdf

Research focused on protein folding, misfolding, and aggregation is leading to major advances across biochemistry and medicine. The elucidation of a folding code is proving to be of extreme importance in the postgenomic era, where a number of orphan genes have been identified for which no clear function has yet been established. This research is starting to shed light on the molecular and biochemical basis of a number of neurodegenerative diseases of dramatic impact. Protein Misfolding in Neurodegenerative Diseases: Mechanisms and Therapeutic Strategies addresses key issues concerning protein misfolding and aggregation in neurodegenerative diseases. Building on recent developments, including the recognition of protein misfolding as both a marker and a causal agent, the text presents the work of those who are actively pursuing more effective treatments, as well as preventative measures, and a possible cure. These include the use of molecular chaperones to control misfolding and novel pharmaceuticals, as well as the potential role of various inhibitors and NSAIDS. A Comprehensive Multifaceted Examination of the Complex Causal Agents Implicated in Protein Misfolding Divided into five sections, this groundbreaking text provides up-to-date accounts for Alzheimer’s, Parkinson’s, Huntington’s, Amyotrophic Lateral Sclerosis and Transmissible Spongiform Encephalitis. It also explores the highly likelihood that multiple factors, including oxidative stress, play a role in these complex diseases.

Author : Vladimir Uversky,Yuri Lyubchenko
Publisher : Academic Press
Page : 552 pages
File Size : 42,8 Mb
Release : 2013-11-05
Category : Technology & Engineering
ISBN : 9780123978219

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Bio-nanoimaging by Vladimir Uversky,Yuri Lyubchenko Pdf

Bio-Nanoimaging: Protein Misfolding & Aggregation provides a unique introduction to both novel and established nanoimaging techniques for visualization and characterization of misfolded and aggregated protein species. The book is divided into three sections covering: - Nanotechnology and nanoimaging technology, including cryoelectron microscopy of beta(2)-microglobulin, studying amyloidogensis by FRET; and scanning tunneling microscopy of protein deposits - Polymorphisms of protein misfolded and aggregated species, including fibrillar polymorphism, amyloid-like protofibrils, and insulin oligomers - Polymorphisms of misfolding and aggregation processes, including multiple pathways of lysozyme aggregation, misfolded intermediate of a PDZ domain, and micelle formation by human islet amyloid polypeptide Protein misfolding and aggregation is a fast-growing frontier in molecular medicine and protein chemistry. Related disorders include cataracts, arthritis, cystic fibrosis, late-onset diabetes mellitus, and numerous neurodegenerative diseases like Alzheimer's and Parkinson's. Nanoimaging technology has proved crucial in understanding protein-misfolding pathologies and in potential drug design aimed at the inhibition or reversal of protein aggregation. Using these technologies, researchers can monitor the aggregation process, visualize protein aggregates and analyze their properties. Provides practical examples of nanoimaging research from leading molecular biology, cell biology, protein chemistry, biotechnology, genetics, and pharmaceutical labs Includes over 200 color images to illustrate the power of various nanoimaging technologies Focuses on nanoimaging techniques applied to protein misfolding and aggregation in molecular medicine

Author : Tony R. Obalinsky
Publisher : Nova Publishers
Page : 294 pages
File Size : 52,5 Mb
Release : 2006
Category : Protein folding
ISBN : 1594548358

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Protein Folding by Tony R. Obalinsky Pdf

Proteins are one of the most basic components of all living cells and therefore serve a vital purpose in the cells of animals, plants and bacteria. They are comprised of chains of amino acids, which are held together by ribosome. These chains have many different patterns, which are known as `folds.' These folds are complicated, and therefore susceptible to irregularities that are known to be the source of many diseases. Cystic fibrosis, mad cow disease, Alzheimer's disease, emphysema and others are all initiated by improper protein folds. It is clear that, improving our understanding of protein folding is a key to fighting these diseases. This book presents recently performed research from around the world on this important subject.

Author : Rossen Donev
Publisher : Academic Press
Page : 452 pages
File Size : 43,6 Mb
Release : 2020-01-13
Category : Science
ISBN : 9780128177518

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Protein Misfolding by Rossen Donev Pdf

Protein Misfolding, Volume 118, covers the wide spectrum of diseases and disorders that are attributed to protein misfolding, including degenerative and neurodegenerative, cardiovascular, renal, glaucoma, cancer, cystic fibrosis, Gaucher's disease, and many others. Specific chapters cover Mass spectrometric approaches for profiling protein folding and stability, Biomembranes, a key player in protein misfolding, how Genetic and environmental factors interact to disrupt proteostasis and trigger protein misfolding diseases, Formation of oligomers and large amorphous aggregates by intrinsically disordered proteins, Protein misfolding in ER stress with applications to cardiovascular and renal disease, and much more. Integrates methods for studying protein misfolding, factors that trigger this process and its role in a wide spectrum of diseases and disorders Contains timely chapters written by well-renowned authorities in their field Provides data that is well supported by a number of high quality illustrations, figures and tables, and targets a very wide audience of specialists, researchers and students

Author : Peter Bross,Niels Gregersen
Publisher : Springer Science & Business Media
Page : 317 pages
File Size : 40,7 Mb
Release : 2008-02-02
Category : Science
ISBN : 9781592593941

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Protein Misfolding and Disease by Peter Bross,Niels Gregersen Pdf

For decades it has been known that structured conformations are important for the proper functioning of most cellular proteins. However, appreciation that protein folding to the functional conformations as well as the structural maintenance of protein molecules are very complex processes has only emerged during the last ten years. The intimate interplay uncovered by this scientific development led us to realize that perturbations of the protein folding process and disturbances of conformational maintenance are major disease mechanisms. This development has given rise to the concept of conformational diseases and the broader signature of protein folding diseases, comprising diseases in which mutations or environmental stresses may result in a partial misfolding that leads then to alternative conformations capable of disturbing cellular processes. This may happen by self-association (aggregation), as in prion and Alzheimer’s diseases, or by incorporation of alternatively folded subunits into structural entities, as in collagen diseases. Another possibility is that folding to the native structure is impaired or abolished, resulting in decreased stea- state levels of the correctly folded protein, as is observed in cystic fibrosis and 1-antitrypsin deficiency, as well as in many enzyme deficiencies. In addition, deficiencies of proteins that are engaged in assisting and supervising protein folding (protein quality control) may impair the folding of many other proteins, resulting in pathological phenotypes. Examples of this are the spastic paraplegia attributable to mutations in mitochondrial protease/chaperone complexes.

Author : Yuan Jian-min,Zhou Huan-xiang
Publisher : World Scientific
Page : 328 pages
File Size : 40,6 Mb
Release : 2017-06-02
Category : Science
ISBN : 9789813202399

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Biophysics And Biochemistry Of Protein Aggregation: Experimental And Theoretical Studies On Folding, Misfolding, And Self-assembly Of Amyloidogenic Peptides by Yuan Jian-min,Zhou Huan-xiang Pdf

This book reviews current research on the important processes involved in neurodegenerative diseases (e.g. Alzheimer's disease) and the peptides and proteins involved in the amyloidogenic processes. It covers the design and developments of anti-amyloid inhibitors, and gives readers a fundamental understanding of the underlying oligomerization and aggregation processes of these diseases from both computational and experimental points of view.

Author : Vladimir Nikolaevič Uverskij,Anthony L. Fink
Publisher : Unknown
Page : 128 pages
File Size : 46,5 Mb
Release : 2006
Category : Cell aggregation
ISBN : OCLC:712022509

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Protein Misfolding, Aggregation and Conformational Diseases by Vladimir Nikolaevič Uverskij,Anthony L. Fink Pdf

Author : Jesus Avila,Naruhiko Sahara
Publisher : Frontiers E-books
Page : 114 pages
File Size : 54,8 Mb
Release : 2014-08-18
Category : Medicine (General)
ISBN : 9782889192618

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Tau oligomers by Jesus Avila,Naruhiko Sahara Pdf

Neurofibrillary tangles (NFTs) composed of intracellular aggregates of tau protein are a key neuropathological feature of Alzheimer’s Disease (AD) and other neurodegenerative diseases, collectively termed tauopathies. The abundance of NFTs has been reported to correlate positively with the severity of cognitive impairment in AD. However, accumulating evidences derived from studies of experimental models have identified that NFTs themselves may not be neurotoxic. Now, many of tau researchers are seeking a “toxic” form of tau protein. Moreover, it was suggested that a “toxic” tau was capable to seed aggregation of native tau protein and to propagate in a prion-like manner. However, the exact neurotoxic tau species remain unclear. Because mature tangles seem to be non-toxic component, “tau oligomers” as the candidate of “toxic” tau have been investigated for more than one decade. In this topic, we will discuss our consensus of “tau oligomers” because the term of “tau oligomers” [e.g. dimer (disulfide bond-dependent or independent), multimer (more than dimer), granular (definition by EM or AFM) and maybe small filamentous aggregates] has been used by each researchers definition. From a biochemical point of view, tau protein has several unique characteristics such as natively unfolded conformation, thermo-stability, acid-stability, and capability of post-translational modifications. Although tau protein research has been continued for a long time, we are still missing the mechanisms of NFT formation. It is unclear how the conversion is occurred from natively unfolded protein to abnormally mis-folded protein. It remains unknown how tau protein can be formed filaments [e.g. paired helical filament (PHF), straight filament and twisted filament] in cells albeit in vitro studies confirmed tau self-assembly by several inducing factors. Researchers are still debating whether tau oligomerization is primary event rather than tau phosphorylation in the tau pathogenesis. Inhibition of either tau phosphorylation or aggregation has been investigated for the prevention of tauopathies, however, it will make an irrelevant result if we don’t know an exact target of neurotoxicity. It is a time to have a consensus of definition, terminology and methodology for the identification of “tau oligomers”.

Author : Cláudio M. Gomes,Patrícia F.N. Faísca
Publisher : Springer
Page : 63 pages
File Size : 50,9 Mb
Release : 2019-02-25
Category : Science
ISBN : 9783319008820

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Protein Folding by Cláudio M. Gomes,Patrícia F.N. Faísca Pdf

This snapshot volume is designed to provide a smooth entry into the field of protein folding. Presented in a concise manner, each section introduces key concepts while providing a brief overview of the relevant literature. Outlook subsections will pinpoint specific aspects related to emerging methodologies, concepts and trends.

Author : Matthias Gaestel
Publisher : Springer Science & Business Media
Page : 464 pages
File Size : 48,9 Mb
Release : 2005-09-27
Category : Science
ISBN : 3540258752

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Molecular Chaperones in Health and Disease by Matthias Gaestel Pdf

Molecular chaperones are involved in a wide variety of essential cellular processes in living cells. A subset of molecular chaperones have been initially described as heat shock proteins protecting cells from stress damage by keeping cellular proteins in a folding competent state and preventing them from irreversible aggregation. Later it became obvious that molecular chaperones are also expressed constitutively in the cell and are involved in complex processes such as protein synthesis, intracellular protein transport, post-translational modification and secretion of proteins as well as receptor signalling. Hence, it is not surprising that molecular chaperones are implicated in the pathogenesis of many relevant diseases and could be regarded as potential pharmacological targets. Starting with the analysis of the mode of action of chaperones at the molecular, cellular and organismic level, this book will then describe specific aspects where modulation of chaperone action could be of pharmacological and therapeutic interest.