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

Stepan S. Denisov; Johannes H. Ippel; Ben J. Mans; Ingrid Dijkgraaf; Tilman M. Hackeng

doi:10.1039/C8CC08777F

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

Stepan S. Denisov,

^a Johannes H. Ippel,

^a Ben J. Mans,

^bc Ingrid Dijkgraaf

‡^a and Tilman M. Hackeng

‡*^a

Author affiliations

* Corresponding authors

^a Department of Biochemistry, University of Maastricht, Cardiovascular Research Institute Maastricht (CARIM), Universiteitssingel 50, Maastricht, The Netherlands
E-mail: t.hackeng@maastrichtuniversity.nl

^b Epidemiology, Parasites and Vectors, Agricultural Research Council-Onderstepoort Veterinary Institute, Onderstepoort 0110, South Africa

^c Department of Life and Consumer Sciences, University of South Africa, South Africa

Abstract

Selenocysteine scanning (SecScan) is a novel technique to map disulfide networks in proteins independent of structure-based distance information and mass spectrometry. SecScan applies systematic substitution of single Cys by Sec in combination with NMR spectroscopy for reliable and unambiguous determination of disulfide bond networks.

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Supplementary files

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Article information

DOI: https://doi.org/10.1039/C8CC08777F
Article type: Communication
Submitted: 03 Nov 2018
Accepted: 28 Nov 2018
First published: 28 Nov 2018

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Chem. Commun., 2019,55, 1374-1377

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

S. S. Denisov, J. H. Ippel, B. J. Mans, I. Dijkgraaf and T. M. Hackeng, Chem. Commun., 2019, 55, 1374 DOI: 10.1039/C8CC08777F

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Chemical Communications

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

Abstract

Supplementary files

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

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