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Functional Disulphide Bonds: Methods and Protocols Second Edition 2026 [Kõva köide]

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  • Formaat: Hardback, 4 pages, kõrgus x laius: 254x178 mm, 100 Illustrations, color; 12 Illustrations, black and white
  • Sari: Methods in Molecular Biology
  • Ilmumisaeg: 27-Apr-2026
  • Kirjastus: Humana
  • ISBN-10: 1071651579
  • ISBN-13: 9781071651575
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Functional Disulphide Bonds: Methods and Protocols Second Edition 2026Suurem pilt
  • Formaat: Hardback, 4 pages, kõrgus x laius: 254x178 mm, 100 Illustrations, color; 12 Illustrations, black and white
  • Sari: Methods in Molecular Biology
  • Ilmumisaeg: 27-Apr-2026
  • Kirjastus: Humana
  • ISBN-10: 1071651579
  • ISBN-13: 9781071651575
Teised raamatud teemal:
Püsilink: https://www.kriso.ee/db/9781071651575.html
This second edition details new and updated techniques used to study disulfide bonds. Chapters guide readers through how disulfide bonds are classified, techniques used to study functional disulfides, allosteric disulfide bonds, and examples of how labile disulfide bonds are employed for new diagnostics and therapeutics. 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, Functional Disulphide Bonds: Methods and Protocols, Second Edition serves as a vital guide to this evolving area of study.
Classification of Disulfide Bonds.- Structural Analysis of Disulfide
Bonds in the RCSB Protein Data Bank Using proteusPy.- Assessing the
Evolutionary Conservation of Protein Disulfide Bonds.- Estimate of Numbers of
Disulfide-Bonded Protein States.- Using AlphaFold3 for the Interrogation of
Protein Disulfide Bonds.- Replacing Cysteine with Selenocysteine: Biochemical
Considerations, Computational Modelling, and Protein Engineering
Applications.- Quantification of the Redox State of Protein Disulfide Bonds.-
Quantification of Site-Specific Disulfide Bond Redox States in Proteins by
Parallel Reaction Monitoring-Mass Spectrometry (PRM-MS).- Identification of
Target Disulphide Bonds Using Mechanism-Based Kinetic Trapping Combined with
Differential Cysteine Labelling.- Quantification of the Redox State of
Integrin Disulfide Bonds.- Identification of Protein Cysteine Modifications
Using Un-Biased Mass Spectrometry-based Proteomics.- Mapping Protein
Disulfide Bonds by Mass Spectrometry.- Determining the Redox Potential of a
Protein Disulfide Bond.- Oxidative Protein Folding Using
trans-3,4-Dihydroxyselenolane Oxide.- Method for Selection of Antithrombin
Disulfide-Bonded Subsets.- Polyclonal Antibody Selection of Partially
Disulfide-Bonded Protein States.- Dynamic Force Spectroscopy for Analysis of
Multiple Disulfide-Bonded Protein States.- Assays of Thiol Isomerase
Activity.- Probing the Mechano-Redox Control of Cell Movement Using
Microfluidic Assays.- Flow Cytometry Assessment of Procoagulant Platelets
Using a Dithiol-Reactive Probe.- Preparation of a Dithiol-Reactive Probe for
PET Imaging of Cell Death.