Communications Chemistry (Sep 2021)

The anatomy of unfolding of Yfh1 is revealed by site-specific fold stability analysis measured by 2D NMR spectroscopy

  • Rita Puglisi,
  • Gogulan Karunanithy,
  • D. Flemming Hansen,
  • Annalisa Pastore,
  • Piero Andrea Temussi

DOI
https://doi.org/10.1038/s42004-021-00566-3
Journal volume & issue
Vol. 4, no. 1
pp. 1 – 9

Abstract

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Solution NMR provides an information-rich technique to monitor the unfolding process and probe the heterogeneity of protein unfolding. Differences in unfolding dynamics of core and peripheral residues during the cold denaturation of Yfh1 are followed in the present study by 1H-15N HSQC spectroscopy.