Force-clamp spectroscopy of single-protein monomers reveals the individual unfolding and folding pathways of I27 and ubiquitin.

@article{GarciaManyes2007ForceclampSO,
  title={Force-clamp spectroscopy of single-protein monomers reveals the individual unfolding and folding pathways of I27 and ubiquitin.},
  author={Sergi Garcia-Manyes and Jasna Bruji{\'c} and Carmen L. Badilla and Juan Manuel Fern{\'a}ndez},
  journal={Biophysical journal},
  year={2007},
  volume={93 7},
  pages={
          2436-46
        }
}
Single-protein force experiments have relied on a molecular fingerprint based on tethering multiple single-protein domains in a polyprotein chain. However, correlations between these domains remain an issue in interpreting force spectroscopy data, particularly during protein folding. Here we first show that force-clamp spectroscopy is a sensitive technique that provides a molecular fingerprint based on the unfolding step size of four single-monomer proteins. We then measure the force-dependent… CONTINUE READING

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