A single-molecule assay to directly identify solvent-accessible disulfide bonds and probe their effect on protein folding.

@article{Ainavarapu2008ASA,
  title={A single-molecule assay to directly identify solvent-accessible disulfide bonds and probe their effect on protein folding.},
  author={Sri Rama Koti Ainavarapu and Arun P. Wiita and Hector Han-Li Huang and J. M. Fern{\'a}ndez},
  journal={Journal of the American Chemical Society},
  year={2008},
  volume={130 2},
  pages={436-7}
}
Disulfide bonds are ubiquitous in proteins. According to a recent survey, there are 97 741 disulfide bonds in 121 779 protein structures available in the Protein Data Bank (PDB). 1 Native2,3 as well as engineered 4-6 disulfide bonds have been shown to control the stability and function of proteins. The redox state of protein disulfide bonds in vivo… CONTINUE READING