During oxidative folding, the formation of disulfide bonds has profound effects on guiding the
protein folding pathway. Until now, comparatively little is known about the changes in the
conformational dynamics in folding intermediates of proteins that contain only a subset of
their native disulfide bonds. In this comprehensive study, we probe the conformational
landscape of non-native states of lysozyme containing a single native disulfide bond utilizing
nuclear magnetic resonance (NMR) spectroscopy, small-angle X-ray scattering (SAXS) …