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Oxidative folding of peptides and proteins /
The formation of disulfide bonds is probably the most influential modification of peptides and proteins. An elaborate set of cellular machinery exists to catalyze and guide this process. In recent years, significant developments have been made in both our understanding of the in vivo situation and t...
| Other Authors: | , |
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| Format: | Printed Book |
| Language: | English |
| Published: |
Cambridge :
Royal Society of Chemistry,
c2009.
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| Series: | RSC biomolecular sciences.
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| Subjects: |
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| 020 | |a 9780854041480 (hbk.) | ||
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| 082 | 0 | 4 | |a 572.633 |2 22 |
| 084 | |a CHE 806f |2 stub | ||
| 084 | |a CHE 820f |2 stub | ||
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| 245 | 0 | 0 | |a Oxidative folding of peptides and proteins / |c edited by Johannes Buchner and Luis Moroder. |
| 260 | |a Cambridge : |b Royal Society of Chemistry, |c c2009. | ||
| 300 | |a xxi, 429 pages : |b illustrations (some color) ; |c 24 cm. | ||
| 490 | 1 | |a RSC biomolecular sciences | |
| 504 | |a Includes bibliographical references and index. | ||
| 505 | 0 | |a Thioredoxins and the regulation of redox conditions in prokaryotes / Carsten Berndt and Arne Holmgren -- Disulfide-bond formation and isomerization in prokaryotes / Goran Malojčić and Rudi Glockshuber -- The periplasm of E. coli : oxidative folding of recombinant proteins / Katharina M. Gebendorfter and Jeannette Winter -- Oxidative protein folding in mitochondria / Kail Hell and Walter Neupert -- Oxidative folding in the endoplasmic reticulum / Seema Chakravarthi, Catherine E. Jessop and Neil J. Bulleid -- The Ero1 sulfhydryl oxidase and the oxidizing potential of the endoplasmic reticulum / Deborah Fass and Carolyn S. Sevier -- Eukaryotic protein disulfide-isomerases and their potential in the production of disulfide-bonded protein products : what we need to know but do not! / Robert B. Freedman -- Cellular responses to oxidative stress / Marianne Ilbert, Caroline Kumsta and Ursula Jakob -- The role of disulfide bonds in protein folding and stability / Matthias Johannes Feige and Johannes Buchner -- Strategies for the oxidative in vitro refolding of disulfide-bridge-containing proteins / Rainer Rudolph and Christian Lange -- Redox potentials of cysteine residues in peptides and proteins : methods for their determination / Dallas L. Rabenstein -- Engineered disulfide bonds for protein design / Luis Moroder, Hans-Jürgen Musiol and Christian Renner -- Selenocysteine as a probe of oxidative protein folding / Joris Beld, Kenneth J. Woycechowsky and Donald Hilvert -- Oxidative folding of single-stranded disulfide-rich peptides / Grzegorz Bulaj and Aleksandra Walewska -- Regioselective disulfide formation / Knut Adermann and Kleomenis Barlos -- Folding motifs of cystine-rich peptides / Norelle L. Daly and David J. Craik -- Double-stranded cystine peptides / John D. Wade -- Multiple-strand cystine peptides / Marion G. Götz, Hans-Jürgen Musiol and Luis Moroder -- Cystine-based scaffolds for functional miniature proteins / Rudolf K. Allemann -- Selenocystine peptides : synthesis, folding and applications / Markus Muttenthaler and Paul F. Alewood. | |
| 520 | |a The formation of disulfide bonds is probably the most influential modification of peptides and proteins. An elaborate set of cellular machinery exists to catalyze and guide this process. In recent years, significant developments have been made in both our understanding of the in vivo situation and the in vitro manipulation of disulfide bonds. This is the first monograph to provide a comprehensive overview of this exciting and rapidly developing area. It offers in-depth insights into the mechanisms of in vivo and in vitro oxidative folding of proteins as well as mono- and multiple-stranded peptides. Procedures applied for laboratory and industrial purposes are also discussed by top experts in the field. |b The book describes the enzymes involved in the correct oxidative folding of cysteine-containing proteins in prokaryotes and eukaryotes. It then goes on to discuss the mimicking of these enzymes for successful in vitro folding of proteins (including synthetic replicates) and to deal with important issues concerning cysteine-rich peptides. The ability of natural bioactive peptides to fold correctly, and in high yields, to form defined structural motifs using cysteine sequence patterns is still puzzling. With this in mind, synthetic procedures for establishing native cysteine frameworks are discussed using selected examples, such as the potential of selenocysteines. The biotechnological and pharmaceutical relevance of proteins, peptides, their variants and synthetic replicates is continuously increasing. Consequently, this book is invaluable for peptide and protein chemists involved in related research and production. | ||
| 650 | 0 | |a Protein folding. | |
| 700 | 1 | |a Moroder, Luis. | |
| 700 | 1 | |a Buchner, Johannes, | |
| 942 | |c BK | ||
| 830 | 0 | |a RSC biomolecular sciences. | |
| 906 | |a 7 |b cbc |c copycat |d 3 |e ncip |f 20 |g y-gencatlg | ||
| 955 | |b hf07 2014-08-26 z-processor |i hf07 2014-08-27 to BCCD | ||
| 955 | |b hf04 2014-07-03 z-processor ON ORDER | ||
| 952 | |0 0 |1 0 |2 ddc |4 0 |6 572_633000000000000_BUC_O |7 0 |9 395315 |a LIF |b LIF |c ST1 |d 2019-09-27 |e Bookshop / Calicut Books |g 9154.67 |i 2884 |l 0 |o 572.633 BUC/O |p LIF2884 |r 2019-10-03 |y REF | ||