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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.
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.
With contributions from experts in the field, this book provides a comprehensive overview of the oxidative folding of cysteine-rich peptides.
In Protein Stability and Folding: Theory and Practice, world-class scientists present in a single volume a comprehensive selection of hands-on recipes for all of the major techniques needed to understand the conformational stability of proteins, as well as their three-dimensional folding. The distinguished contributors provide clear, step-by-step instructions along with many troubleshooting tips, alternative procedures, and informative explanations about why certain steps are necessary. Even highly skilled researchers will find many time-saving methods. Among the techniques discussed are fluorescent, ultraviolet, and infrared spectroscopy; HPLC peptide mapping; differential scanning calorimetry; and hydrogen exchange. Shirley's Protein Stability and Folding: Theory and Practice will ensure a significant difference in the outcome of your experiments, producing the result desired even for beginners.
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
Pancreatic ribonuclease, the focus of highly productive scientific research for more than half a century and the only enzyme to be the basis of four Nobel prizes, has recently undergone a resurgence in popularity for the recognition of an extended ribonuclease superfamily with functions ranging from tumour growth and inhibition to self-recognition and neurotoxicity. This volume highlights the functional diversity of ribonucleases and reveals the emerging research opportunities provided by these enzymes. * Never before has discussion of the entire family of ribonucleases and related enzymes been covered in a single volume* Core chapters focus on the latest structures and functions of pancreatic-type ribonucleases* Structures and functions of intracellular ribonucleases and nondigestive members of the family are also covered* How ribonucleases continue to serve as excellent systems with which to uncover the secrets of protein chemistry is demonstrated
The second edition of this encyclopedia presents over 400 biologically important signaling molecules and the content is built on the core concepts of their functions along with early findings written by some of the world’s foremost experts. The molecules are described by recognized leaders in each molecule. The interactions of these single molecules in signal transduction networks will also be explored. This encyclopedia marks a new era in overview of current cellular signaling molecules for the specialist and the interested non-specialist alike. Currently, there are more than 30,000 genes in human genome. However, not all the proteins encoded by these genes work equally in order to maintain homeostasis. Understanding the important signaling molecules as completely as possible will significantly improve our research-based teaching and scientific capabilities.
This book will deal with heat shock proteins and more generally with stress-related inducible gene expression as a pleiotropic adaptive response to stress. It presents a textbook-like overview of the field not only to heat shock experts, but to physiologists, pharmacologists, physicians, neuropsychologists and others as well. It is intended to be a state-of-the-art and perspective book rather than an up-to-date presentation of recent data. It should provide a basis for new experimental approaches to fields at the edge of the classical heat shock field. Drugs, UV irradiation and environmental toxics will considered as important modulators of the stress response. Radical scavengers such as superoxide dismutases and inducible regulatory proteins of metallic ion status such as ferritin as well as immunophilins and protein disulfide isomerases will be considered within the frame of stress proteins. The potential practical applications of heat shock proteins in toxicology and medicine for the diagnosis, prognosis and eventually therapy of clinical conditions associated with an increased oxidative burden will be outlined. The role of heat shock proteins in the modulation of immune responses will also be included. The book considers heat shock from a broad perspective including fields for which heat-shock may become of importance in the very near future such as cellular responses to environmental stresses and complex stress responses under specific conditions. It was also felt timely to incorporate a whole section on medical and technological applications of stress proteins.
Protein Folding aims to collect the most important information in the field of protein folding and probes the main principles that govern formation of the three-dimensional structure of a protein from a nascent polypeptide chain, as well as how the functional properties appear. This text is organized into three sections and consists of 15 chapters. After an introductory chapter where the main problems of protein folding are considered at the cellular level in the context of protein biosynthesis, the discussion turns to the conformation of native globular proteins. Definitions and rules of nomenclature are given, including the structural organization of globular proteins deduced from X-ray crystallographic data. Folding mechanisms are tentatively deduced from the observation of invariants in the architecture of folded proteins. The next chapters focus on the energetics of protein conformation and structure, indicating the principles of thermodynamic stability of the native structure, along with theoretical computation studies of protein folding, structure prediction, and folding simulation. The reader is also introduced to various experimental approaches; the reversibility of the unfolding-folding process; equilibrium and kinetic studies; and detection and characterization of intermediates in protein folding. This text concludes with a chapter dealing with problems specific to oligomeric proteins. This book is intended for research scientists, specialists, biochemists, and students of biochemistry and biology.