Oxidative folding pathways of bovine milk β-lactoglobulin with odd cysteine residues.

ABSTRACT: Bovine β-lactoglobulin (BLG) is a major whey protein with unique structural characteristics: it possesses a free Cys thiol (SH) and two disulfide (SS) bonds and consists of a β-barrel core surrounded by one long and several short α helices. Although SS-intact conformational folding has been studied in depth, the oxidative folding pathways and accompanying SS formation/rearrangement are poorly understood. In this study, we used trans-3,4-dihydroxyselenolane oxide, a water-soluble selenoxide reagent which undergoes rapid and quantitative SS formation, to determine the oxidative folding pathways of BLG variant A (BLGA) at pH 8.0 and 25 °C. This was done by characterizing two key one-SS intermediates, a particular folding intermediate having a Cys66-Cys160 SS bond (I-1) and a particular foldin

SUBMITTER: Iwaoka M 

PROVIDER: S-EPMC6668375 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature