Oxidative Folding Of Proteins
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Author | : Luis Moroder |
Publisher | : Royal Society of Chemistry |
Total Pages | : 453 |
Release | : 2009 |
Genre | : Science |
ISBN | : 0854041486 |
With contributions from experts in the field, this book provides a comprehensive overview of the oxidative folding of cysteine-rich peptides.
Author | : Matthias J Feige |
Publisher | : Royal Society of Chemistry |
Total Pages | : 450 |
Release | : 2018-07-30 |
Genre | : Science |
ISBN | : 1782629904 |
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.
Author | : Rowen J. Y. Chang |
Publisher | : Springer Science & Business Media |
Total Pages | : 290 |
Release | : 2011-08-12 |
Genre | : Science |
ISBN | : 1441972730 |
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.
Author | : Benjamin Peng-Chu Tu |
Publisher | : |
Total Pages | : 246 |
Release | : 2003 |
Genre | : |
ISBN | : |
Author | : Howard J. Leung |
Publisher | : |
Total Pages | : 56 |
Release | : 2005 |
Genre | : |
ISBN | : |
Author | : Roger H. Pain |
Publisher | : |
Total Pages | : 296 |
Release | : 1994 |
Genre | : Science |
ISBN | : |
The past five years have seen a major leap forward in our understanding of the way proteins fold into their three-dimensional, functional conformations. The rapidly expanding literature covers in vivo as well as in vitro studies and forms the basis for an important biotechnology industry. In this volume, a group of leading scientists review and assess the experimental evidence that underpins these advances and look for signs of a general picture of how proteins fold. Contributors show how such conformational changes are leading to new insights into membrane translocation, pore formation, and the clinically important aggregation phenomena. Students and researchers of biochemistry and molecular biology will find this book to be the ideal introduction to an exciting field.
Author | : |
Publisher | : John Wiley & Sons |
Total Pages | : 508 |
Release | : 2013-02-13 |
Genre | : Science |
ISBN | : 3527631852 |
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
Author | : Julianne Zedalis |
Publisher | : |
Total Pages | : 1923 |
Release | : 2017-10-16 |
Genre | : Biology |
ISBN | : 9781947172401 |
Biology for AP® courses covers the scope and sequence requirements of a typical two-semester Advanced Placement® biology course. The text provides comprehensive coverage of foundational research and core biology concepts through an evolutionary lens. Biology for AP® Courses was designed to meet and exceed the requirements of the College Board’s AP® Biology framework while allowing significant flexibility for instructors. Each section of the book includes an introduction based on the AP® curriculum and includes rich features that engage students in scientific practice and AP® test preparation; it also highlights careers and research opportunities in biological sciences.
Author | : Marina Ramirez-Alvarado |
Publisher | : John Wiley & Sons |
Total Pages | : 1311 |
Release | : 2010-12-01 |
Genre | : Science |
ISBN | : 1118031814 |
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 | : Jesus Avila |
Publisher | : Frontiers E-books |
Total Pages | : 114 |
Release | : 2014-08-18 |
Genre | : Medicine (General) |
ISBN | : 288919261X |
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”.