Rapid Disulfide Mapping in Peptides and Proteins by meta-Chloroperoxybenzoic Acid (mCPBA) Oxidation and Tandem Mass Spectrometry-Reference-Cited by-同舟云学术

Rapid Disulfide Mapping in Peptides and Proteins by meta-Chloroperoxybenzoic Acid (mCPBA) Oxidation and Tandem Mass Spectrometry

Published:2021-10-27 Issue:44 Volume:93 Page:14618-14625
ISSN:0003-2700
Container-title:Analytical Chemistry
language:en
Short-container-title:Anal. Chem.

Author:

Zhao Xu¹,Zhang Sichun¹^ORCID,Ma Qiang²^ORCID,Zhang Xinrong¹,Ma Xiaoxiao³^ORCID

Affiliation:

1. Department of Chemistry, Tsinghua University, Beijing 100084, China

2. Chinese Academy of Inspection and Quarantine, Beijing 100176, China

3. State Key Laboratory of Precision Measurement Technology and Instruments, Department of Precision Instrument, Tsinghua University, Beijing 100084, China

Funder

National Natural Science Foundation of China

Publisher

American Chemical Society (ACS)

Subject

Analytical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.analchem.1c02379

Reference43 articles.

1. Substantial increase of protein stability by multiple disulphide bonds

2. Disulfide Bonding in Protein Biophysics

3. Multifaceted Roles of Disulfide Bonds. Peptides as Therapeutics

4. Protein disulfide bond determination by mass spectrometry

5. A novel salt bridge mechanism highlights the need for nonmobile proton conditions to promote disulfide bond cleavage in protonated peptides under low-energy collisional activation

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