Oxidative Folding of Peptides and Proteins - read free eBook in online reader or directly download on the web page. Select files or add your book in reader. Download and read online ebook Oxidative Folding of Peptides and Proteins write by Luis Moroder. This book was released on 2009. Oxidative Folding of Peptides and Proteins available in PDF, EPUB and Kindle. With contributions from experts in the field, this book provides a comprehensive overview of the oxidative folding of cysteine-rich peptides.
Folding of Disulfide Proteins
Folding of Disulfide Proteins - read free eBook in online reader or directly download on the web page. Select files or add your book in reader. Download and read online ebook Folding of Disulfide Proteins write by Rowen J. Y. Chang. This book was released on 2011-08-12. Folding of Disulfide Proteins available in PDF, EPUB and Kindle. 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.
Biochemical Basis of Oxidative Protein Folding in the Endoplasmic Reticulum
Biochemical Basis of Oxidative Protein Folding in the Endoplasmic Reticulum - read free eBook in online reader or directly download on the web page. Select files or add your book in reader. Download and read online ebook Biochemical Basis of Oxidative Protein Folding in the Endoplasmic Reticulum write by Benjamin Peng-Chu Tu. This book was released on 2003. Biochemical Basis of Oxidative Protein Folding in the Endoplasmic Reticulum available in PDF, EPUB and Kindle.
Protein Folding in the Cell
Protein Folding in the Cell - read free eBook in online reader or directly download on the web page. Select files or add your book in reader. Download and read online ebook Protein Folding in the Cell write by . This book was released on 2002-02-20. Protein Folding in the Cell available in PDF, EPUB and Kindle. 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.
Oxidative Protein Folding in Vitro
Oxidative Protein Folding in Vitro - read free eBook in online reader or directly download on the web page. Select files or add your book in reader. Download and read online ebook Oxidative Protein Folding in Vitro write by Pumtiwitt C. Rancy. This book was released on 2010. Oxidative Protein Folding in Vitro available in PDF, EPUB and Kindle. Oxidative protein folding describes the process by which disulfide bonds are inserted into proteins as they fold into their native structure. This involves two distinct phases, an oxidation phase where these covalent linkages are first introduced, and an isomerization phase in which incorrectly placed disulfides are shuffled leading to the native pairings. In eukaryotes, disulfide bond formation can be catalyzed by a number of flavin-dependent sulfhydryl oxidases. This dissertation work investigates how a particular flavin-dependent sulfhydryl oxidase, Quiescin-sulfhydryl oxidase (QSOX), cooperates with protein disulfide isomerase (PDI) to generate native pairings in two unfolded reduced proteins: ribonuclease A (RNase A, four disulfide bonds and 105 disulfide isomers of the fully oxidized protein) and avian riboflavin binding protein (RfBP, nine disulfide bonds and more than 34 million corresponding disulfide pairings). This QSOX/PDI in vitro folding system involves no functional interaction between the two enzymatic components; QSOX inserts disulfide bonds into protein substrates while PDI isomerizes the misplaced pairs to the native ones. Rapid refolding does not require glutathione or glutathione-based redox buffers. Refolding of RfBP is followed continuously by monitoring spectral changes experienced by the ligand, riboflavin, upon binding to the apoprotein. Efficient refolding of this protein only occurs with a large molar excess of reduced PDI over the folding client protein. These conditions likely mirror the environment of the endoplasmic reticulum lumen where small concentrations of nascent proteins are exposed to nearly mM levels of PDI. Subsequent studies performed in the absence of QSOX or redox buffers, explore the effectiveness of mixtures of oxidized and reduced PDI in refolding RfBP. Here, the fastest refolding of RfBP occurs with excess reduced PDI and just enough oxidized PDI to generate nine disulfides in the protein. The implications of these in vitro experiments for understanding oxidative folding processes in vivo are discussed. Although unfolded proteins have been proven to be excellent substrates of QSOX, a recent proposal suggests that it can also function in the generation of inter-domain and inter-protein disulfide bridges, where the substrates are already substantially or completely folded. This suggestion has been tested using wild type and mutant Escherichia coli thioredoxin as a model substrate. These folded substrates are, by comparison, poorly oxidized by QSOX which is consistent with the expected stringent steric requirements for efficient thiol/disulfide exchange reactions.
