TL;DR
This chapter describes the dynamic force spectroscopy method for analyzing the redox regulation of distinct disulfide-bonded protein conformations and offers a robust framework for examining other disulfide-bonded protein states.
Intramolecular distances existing between the sheets that define the β-barrel fold of BsCspB have been shown to respond nonuniformly to increasing hydrostatic pressure, suggesting that the three-dimensional structure of native BsCspB is modified such that β-strands depart from each other.
The results reveal that the collapse exhibits two-state dynamics between structurally distributed ensembles, occurring on a time scale of tens of microseconds across all variants, indicating a global contraction of the whole protein structure with a substantial free energy barrier.
The fundamental principles of the IM-CIU method are outlined, highlighting its ability to resolve proteins with near-identical collision cross sections, and discussing its potential impact on the development of future pharmaceutical applications.
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