Coverart for item
The Resource Oxidative folding of proteins : basic principles, cellular regulation and engineering, edited by Matthias J. Feige

Oxidative folding of proteins : basic principles, cellular regulation and engineering, edited by Matthias J. Feige

Label
Oxidative folding of proteins : basic principles, cellular regulation and engineering
Title
Oxidative folding of proteins
Title remainder
basic principles, cellular regulation and engineering
Statement of responsibility
edited by Matthias J. Feige
Contributor
Editor
Subject
Language
eng
Summary
With contributions from experts in the field, this book provides a comprehensive overview of the oxidative folding of cysteine-rich proteins
Member of
Cataloging source
N$T
Dewey number
572/.633
Illustrations
illustrations
Index
index present
LC call number
QP551
LC item number
.O85 2018
Literary form
non fiction
Nature of contents
  • dictionaries
  • bibliography
NLM call number
QU 55.9
http://library.link/vocab/relatedWorkOrContributorName
Feige, Matthias J.
Series statement
Chemical biology
Series volume
9
http://library.link/vocab/subjectName
  • Protein folding
  • Protein Folding
  • Molecular biology
  • SCIENCE
  • Protein folding
Label
Oxidative folding of proteins : basic principles, cellular regulation and engineering, edited by Matthias J. Feige
Instantiates
Publication
Antecedent source
unknown
Bibliography note
Includes bibliographical references and index
Carrier category
online resource
Carrier category code
  • cr
Carrier MARC source
rdacarrier
Color
multicolored
Content category
text
Content type code
  • txt
Content type MARC source
rdacontent
Contents
Section 1: Principles and Analysis of Disulfide Bond Formation; Disulfide Bonds in Protein Folding and Stability; Techniques to Monitor Disulfide Bond Formation and the Reduction Potential of Cysteine-Cystine Couples In vitro and In vivo; Real-time Detection of Thiol Chemistry in Single Proteins; Analysis of Disulfide Bond Formation in Therapeutic Proteins; Section 2: Disulfide Bonds in Peptides and Proteins: Structure, Function and Evolution; Evolutionary Adaptations to Cysteine-rich Peptide Folding; In vitro Refolding of Proteins; Allosteric Disulfide Bonds; Section 3: Oxidative Folding in the Cell; Disulfide Bond Formation and Isomerization in Escherichia coli; Disulfide Bond Formation in Mitochondria; Structural Insights into Disulfide Bond Formation and Protein Quality Control in the Mammalian Endoplasmic Reticulum; Mechanisms of Oxidative Protein Folding and Thiol-dependent Quality Control: Tales of Cysteines and Cystines; Disulfide Bond Formation Downstream of the Endoplasmic Reticulum; Section 4: Oxidative Folding and Cellular/Organism Homeostasis; How Microbes Cope with Oxidative Stress; Disulfide Bond Formation in the Endoplasmic Reticulum; Redox Regulation of Hsp70 Chaperone Function in the Endoplasmic Reticulum; Thioredoxin and Cellular Redox Systems: Beyong Protein Disulfide Bond Reduction; Section 5: Engineering Covalent Linkages in Peptides and Proteins; Stabilization of Peptides and Proteins by Engineered Disulfide Bonds; Genetic Code Expansion Approaches to Introduce Artificial Covalent Bonds into Proteins in Vivo
Control code
1048428986
Dimensions
unknown
Extent
1 online resource
File format
unknown
Form of item
online
Isbn
9781788013253
Level of compression
unknown
Media category
computer
Media MARC source
rdamedia
Media type code
  • c
http://library.link/vocab/ext/overdrive/overdriveId
3-178-9781788013253
Quality assurance targets
not applicable
Reformatting quality
unknown
Sound
unknown sound
Specific material designation
remote
System control number
(OCoLC)1048428986
Label
Oxidative folding of proteins : basic principles, cellular regulation and engineering, edited by Matthias J. Feige
Publication
Antecedent source
unknown
Bibliography note
Includes bibliographical references and index
Carrier category
online resource
Carrier category code
  • cr
Carrier MARC source
rdacarrier
Color
multicolored
Content category
text
Content type code
  • txt
Content type MARC source
rdacontent
Contents
Section 1: Principles and Analysis of Disulfide Bond Formation; Disulfide Bonds in Protein Folding and Stability; Techniques to Monitor Disulfide Bond Formation and the Reduction Potential of Cysteine-Cystine Couples In vitro and In vivo; Real-time Detection of Thiol Chemistry in Single Proteins; Analysis of Disulfide Bond Formation in Therapeutic Proteins; Section 2: Disulfide Bonds in Peptides and Proteins: Structure, Function and Evolution; Evolutionary Adaptations to Cysteine-rich Peptide Folding; In vitro Refolding of Proteins; Allosteric Disulfide Bonds; Section 3: Oxidative Folding in the Cell; Disulfide Bond Formation and Isomerization in Escherichia coli; Disulfide Bond Formation in Mitochondria; Structural Insights into Disulfide Bond Formation and Protein Quality Control in the Mammalian Endoplasmic Reticulum; Mechanisms of Oxidative Protein Folding and Thiol-dependent Quality Control: Tales of Cysteines and Cystines; Disulfide Bond Formation Downstream of the Endoplasmic Reticulum; Section 4: Oxidative Folding and Cellular/Organism Homeostasis; How Microbes Cope with Oxidative Stress; Disulfide Bond Formation in the Endoplasmic Reticulum; Redox Regulation of Hsp70 Chaperone Function in the Endoplasmic Reticulum; Thioredoxin and Cellular Redox Systems: Beyong Protein Disulfide Bond Reduction; Section 5: Engineering Covalent Linkages in Peptides and Proteins; Stabilization of Peptides and Proteins by Engineered Disulfide Bonds; Genetic Code Expansion Approaches to Introduce Artificial Covalent Bonds into Proteins in Vivo
Control code
1048428986
Dimensions
unknown
Extent
1 online resource
File format
unknown
Form of item
online
Isbn
9781788013253
Level of compression
unknown
Media category
computer
Media MARC source
rdamedia
Media type code
  • c
http://library.link/vocab/ext/overdrive/overdriveId
3-178-9781788013253
Quality assurance targets
not applicable
Reformatting quality
unknown
Sound
unknown sound
Specific material designation
remote
System control number
(OCoLC)1048428986

Library Locations

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