Oxidative Folding Of Peptides And Proteins

With contributions from experts in the field, this book provides a comprehensive overview of the oxidative folding of cysteine-rich peptides.

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.

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.

In Protein Structure, Stability, and Folding, Kenneth P. Murphy and a panel of internationally recognized investigators describe some of the newest experimental and theoretical methods for investigating these critical events and processes. Among the techniques discussed are the many methods for calculating many of protein stability and dynamics from knowledge of the structure, and for performing molecular dynamics simulations of protein unfolding. New experimental approaches presented include the use of co-solvents, novel applications of hydrogen exchange techniques, temperature-jump methods for looking at folding events, and new strategies for mutagenesis experiments. Unique in its powerful combination of theory and practice, Protein Structure, Stability, and Folding offers protein and biophysical chemists the means to gain a more comprehensive understanding of some of this complex area by detailing many of the major techniques in use today.

The process by which newly synthesized polypeptide chains become their final 3-dimensional protein forms is clearly explained, providing students and researchers of various backgrounds with both a conceptual and technical understanding of the subject. The new Second Edition incorporates the significant improvements in the field such as advances in interpreting observed kinetic data, the development of technology to observe fast folding reactions, the molten globule state, and the vital role of chaperone proteins in protein folding. The emphasis on experimental approaches has been maintained but this edition does so within the explicit context of simulations and energy surfaces. New discoveries of the central importance of protein folding and unfolding reactions in biology and medicine (including mutation and 'misfolding') are carefully explored. Three case studies elucidate the difficulties of studying protein folding in vivo.

Human cells produce at least 30,000 different proteins. Each has a specific function characterized by a unique sequence and native conformation that allows it to perform that function. While research in this post-genomic era has created a deluge of invaluable information, the field has lacked for an authoritative introductory text needed to inform researchers and students in all of those fields now concerned with protein research. Introduction to Peptides and Proteins brings together some of the most respected researchers in protein science to present a remarkably coherent introduction to modern peptide and protein chemistry. The first sections of the book delve into – Basic peptide and protein science from assembly through degradation Traditional and emerging research methods including those used in bioinformatics and proteomics New computational approaches and algorithms used to find patterns in the vast data collected by sequencing projects After providing a foundation in tools and methods, the authors closely examine six protein families, including representative classes such as enzymes, cell-surface receptors, antibodies, fibrous proteins, and bioactive peptide classes. They concentrate on biochemical mechanisms and where possible indicate therapeutic or biotechnical possibilities. Then focusing on clinical aspects, the authors investigate misfolding as found in prion diseases, miscleavage as found in Alzheimer’s, and mis-sequencing as found with some cancers. Drawing from some of their own research, the authors summarize recent achievements and emerging applications. They discuss the use of proteins and peptides as drugs and the solid-phase synthesis required for drug production. They also look at the use of peptides as functional biomolecules and research tools. No longer just the domain of biologists, many key advances in protein research started in physics labs and have involved contributions from a host of fields including statistics, drug development, genetics, and chemical spectroscopy. Introduction to Peptides and Proteins provides researchers across these fields with the thorough foundation needed to explore all the potential that protein research offers.

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.