Jin, J. Min, H. Kwon, O.-S. Oh, H.J. Kim, J. Park, C. 2024-01-20T02:30:51Z 2024-01-20T02:30:51Z 2021-08-31 2017-02 0304-128X https://pubs.kist.re.kr/handle/201004/123167 The determination of disulfide bonds is important for comprehensive understanding of the chemical structure of protein. So far, many strategies for the disulfide bond analysis have been suggested in terms of speed and sensitivity. However, most of these strategies have not considered free thiol residues in the target protein in the process of determining the disulfide bond. We suggested the strategy which was composed of four steps for the identification of disulfide bonds; the first step was the prediction of possible disulfide bonds, the second step was the determination of free cysteine residues, the third step was the analysis of disulfide bond using a high-resolution mass spectrometry, and the final step was the determination of disulfide bonds based on the comprehensive verification. In this study, we performed the characterization of disulfide bonds for the recombinant protein (HRPE1), where 1 and 5 inter- and intra-chain disulfide bonds were identified, respectively. ？ 2017, Korean Institute of Chemical Engineers. All rights reserved. Korean Korean Institute of Chemical Engineers Mass spectrometry-based strategy for effective disulfide bond identification Article 10.9713/kcer.2017.55.1.27 1 Korean Chemical Engineering Research, v.55, no.1, pp.27 - 33 Korean Chemical Engineering Research 55 1 27 33 N scopus kci ART002194294 2-s2.0-85013682610 Article Disulfide bond Free-thiol group Mass spectrometry Peptide mapping