MARC details
| 000 -LEADER |
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| fixed length control field |
03715nam a2200277 a 4500 |
| 001 - ACCESSION NUMBER |
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| control field |
017501981 |
| 003 - CONTROL NUMBER IDENTIFIER |
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| control field |
CUTN |
| 005 - DATE AND TIME OF LATEST TRANSACTION |
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| control field |
20171110150426.0 |
| 008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION |
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| fixed length control field |
080721s2009 enka b 001 0 eng d |
| 020 ## - INTERNATIONAL STANDARD BOOK NUMBER |
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| International Standard Book Number |
9780854041480 |
| Terms of availability |
£99.00 |
| 040 ## - CATALOGING SOURCE |
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| Original cataloging agency |
StDuBDS |
| Language of cataloging |
eng |
| Transcribing agency |
StDuBDS |
| 082 04 - DEWEY DECIMAL CLASSIFICATION NUMBER |
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| Classification number |
572.633 |
| Edition number |
22 |
| Item number |
BUC |
| 245 00 - TITLE STATEMENT |
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| Title |
Oxidative folding of peptides and proteins / |
| Statement of responsibility, etc |
edited by Johannes Buchner and Luis Moroder. |
| 260 ## - PUBLICATION, DISTRIBUTION, ETC. (IMPRINT) |
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| Place of publication, distribution, etc |
Cambridge : |
| Name of publisher, distributor, etc |
Royal Society of Chemistry, |
| Date of publication, distribution, etc |
2009. |
| 300 ## - PHYSICAL DESCRIPTION |
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| Extent |
xxi, 429 p. : |
| Other physical details |
ill. (some col.) ; |
| Dimensions |
24 cm. |
| 490 1# - SERIES STATEMENT |
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| Series statement |
RSC biomolecular sciences |
| 500 ## - GENERAL NOTE |
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| General note |
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. 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 |
| 504 ## - BIBLIOGRAPHY, ETC. NOTE |
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| Bibliography, etc |
Includes bibliographical references and index. |
| 505 ## - FORMATTED CONTENTS NOTE |
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| Formatted contents note |
Preface. Foreword. Chapter 1. Oxidative Folding of Proteins in Vivo: Thioredoxins and the regulation of redox conditions in prokaryotes; Dsb A B; Eucaryotic PDIs; Structure of Ero1/oxidation in the ER; Oxidative folding in the ER; Oxidative protein folding in mitochondria; Cellular responses to redox stress; Harnessing disulfide bond formation in the periplasm of bacteria for recombinant protein production. Chapter 2. Oxidative Folding of Proteins in vitro: The role of disulfide bonds for folding and stability of proteins; Strategies for the oxidative refolding of disulfide-bonded proteins. Chapter 3. Redox potentials of cysteine residues in peptides and proteins: Methods for their determination. Chapter 4. Engineering disulfide bonds. Chapter 5. Selenocysteine as a probe of oxidative protein folding. Chapter 6. Oxidative Folding of Peptides in vitro: Oxidative folding of single-stranded disulfide-rich Peptides; Regioselective disulfide formation; Folding motifs of cysteine-rich peptides; Double-stranded cysteine-peptides; Multiple-strand cysteine-peptides. Chapter 7. Cysteine-based scaffolds for functional miniature proteins. Chapter 8. Selenocystine-peptides - Synthesis, folding and applications. |
| 650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM |
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| Topical term or geographic name as entry element |
Protein folding. |
| 700 1# - ADDED ENTRY--PERSONAL NAME |
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| Personal name |
Moroder, Luis. |
| 700 1# - ADDED ENTRY--PERSONAL NAME |
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| Personal name |
Buchner, Johannes, |
| Titles and other words associated with a name |
Prof. |
| 830 #0 - SERIES ADDED ENTRY--UNIFORM TITLE |
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| Uniform title |
RSC biomolecular sciences. |
| 942 ## - ADDED ENTRY ELEMENTS (KOHA) |
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| Source of classification or shelving scheme |
Dewey Decimal Classification |
| Koha item type |
General Books |
