Functional Disulphide Bonds

1. Front Matter

   Pages i-xi

   PDF

2. Classification of Protein Disulphide Bonds

   • Aster E. Pijning, Philip Hogg

   Pages 1-8

3. Assessing the Evolutionary Conservation of Protein Disulphide Bonds

   • Jason W. H. Wong

   Pages 9-19

4. A Proteomics Workflow for the Identification of Labile Disulphide Bonds at the Cell Surface

   • Clive Metcalfe

   Pages 21-43

5. Quantification of the Redox State of Protein Disulphide Bonds

   • Joyce Chiu

   Pages 45-63

6. Determining the Redox Potential of a Protein Disulphide Bond

   • Kristina M. Cook

   Pages 65-86

7. Studying Functional Disulphide Bonds by Computer Simulations

   • Frauke Gräter, Wenjin Li

   Pages 87-113

8. Dynamic Force Spectroscopy Analysis on the Redox States of Protein Disulphide Bonds

   • Lining Ju

   Pages 115-131

9. Assays of Thiol Isomerase Enzymatic Activity

   • Roelof H. Bekendam, Robert Flaumenhaft

   Pages 133-148

10. Functional Assays of Thiol Isomerase ERp5

    • Alexander Dupuy, Freda Passam

    Pages 149-163

11. Identification of PDI Substrates by Mechanism-Based Kinetic Trapping

    • Oskar Eriksson, Jack Stopa, Bruce Furie

    Pages 165-182

12. Site-Specific Proteomic Mapping of Modified Cysteine Residues

    • Neal S. Gould

    Pages 183-195

13. Quantitation of Glutathione, Glutathione Disulphide, and Protein-Glutathione Mixed Disulphides by High-Performance Liquid Chromatography-Tandem Mass Spectrometry

    • Michael R. Bukowski, Matthew J. Picklo Sr.

    Pages 197-210

14. Interrogation of Functional Mitochondrial Cysteine Residues by Quantitative Mass Spectrometry

    • Daniel W. Bak, Eranthie Weerapana

    Pages 211-227

15. Oxidative Protein Folding Using trans-3,4-Dihydroxyselenolane Oxide

    • Kenta Arai, Michio Iwaoka

    Pages 229-244

16. Methodology for Identification of Cysteine-Reactive Covalent Inhibitors

    • Stefan G. Kathman, Alexander V. Statsyuk

    Pages 245-262

17. In Vivo Measurement of Redox-Regulated TG2 Activity

    • Arek V. Melkonian, Nielson Weng, Brad A. Palanski, Chaitan Khosla

    Pages 263-274

18. Quantitation of Total and Free Thiol β2-Glycoprotein I Levels for Diagnostic and Prognostic Purposes in the Antiphospholipid Syndrome

    • M. Qi, James C. Weaver, S. A. Krilis, B. Giannakopoulos

    Pages 275-283

19. Quantitation of Total and Free Thiol Angiotensinogen as a Prognostic Marker for Preeclampsia

    • M. Qi, James C. Weaver, S. Rahgozar, B. Giannakopoulos, S. A. Krilis

    Pages 285-293

20. Preparation of a Dithiol-Reactive Probe for PET Imaging of Cell Death

    • Ivan Ho Shon, Michael P. Gotsbacher, Jennifer Guille, Divesh Kumar, Rachel Codd, Philip Hogg

    Pages 295-304

This book describes the current techniques used to study functional disulphides and to exploit them for therapeutic outcomes. Beginning with how disulphide bonds are classified and how to study their evolution, the volume then continues with protein chemical, molecular dynamics, and force spectroscopy techniques used to identify functional disulphides and/or study their behavior, then focuses on techniques employed in the study of the factors that cleave and/or form disulphide bonds. Methods to study how particular functional disulphides are assayed in mouse and human tissues are likewise examined, amongst many other subjects. Written for the highly successful Methods in Molecular Biology series, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. 

Authoritative and practical, FunctionalDisulphide Bonds: Methods and Protocols serves as a vital guide to this evolving area of study.

• Polypeptide chains
• Post-translational modification
• Protein function
• Cysteine thiols
• Covalent drugs

• The Centenary Institute, NHMRC Clinical Trials Centre, Sydney Medical School, University of Sydney, Sydney, Australia

  Philip Hogg

Policies and ethics