SecScan: a general approach for mapping disulfide bonds in synthetic and recombinant peptides and proteins-Reference-Cited by-同舟云学术

SecScan: a general approach for mapping disulfide bonds in synthetic and recombinant peptides and proteins

Published:2019 Issue:10 Volume:55 Page:1374-1377
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Denisov Stepan S.¹²³⁴⁵^ORCID,Ippel Johannes H.¹²³⁴⁵^ORCID,Mans Ben J.⁶⁷⁸⁹¹⁰^ORCID,Dijkgraaf Ingrid¹²³⁴⁵^ORCID,Hackeng Tilman M.¹²³⁴⁵^ORCID

Affiliation:

1. Department of Biochemistry

2. University of Maastricht

3. Cardiovascular Research Institute Maastricht (CARIM)

4. Maastricht

5. The Netherlands

6. Epidemiology, Parasites and Vectors

7. Agricultural Research Council-Onderstepoort Veterinary Institute

8. Onderstepoort 0110

9. South Africa

10. Department of Life and Consumer Sciences

Abstract

Selenocysteine scanning (SecScan) is a novel technique to map disulfide networks in proteins independent of structure-based distance information and mass spectrometry.

Funder

Nederlandse Organisatie voor Wetenschappelijk Onderzoek

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2019/CC/C8CC08777F

Reference23 articles.

1. Strategies in mass spectrometry for the assignment of Cys-Cys disulfide connectivities in proteins

2. General Approach To Determine Disulfide Connectivity in Cysteine-Rich Peptides by Sequential Alkylation on Solid Phase and Mass Spectrometry

3. Disulfide structures of highly bridged peptides: A new strategy for analysis

4. Evaluation of disulfide scrambling during the enzymatic digestion of bevacizumab at various pH values using mass spectrometry

5. Combined Use of Ion Mobility and Collision-Induced Dissociation To Investigate the Opening of Disulfide Bridges by Electron-Transfer Dissociation in Peptides Bearing Two Disulfide Bonds

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