Achieving secondary structural resolution in kinetic measurements of protein folding: a case study of the folding mechanism of Trp-cage.

@article{Culik2011AchievingSS,
  title={Achieving secondary structural resolution in kinetic measurements of protein folding: a case study of the folding mechanism of Trp-cage.},
  author={Robert M. Culik and A. Serrano and Michelle R Bunagan and F. Gai},
  journal={Angewandte Chemie},
  year={2011},
  volume={50 46},
  pages={
          10884-7
        }
}
  • Robert M. Culik, A. Serrano, +1 author F. Gai
  • Published 2011
  • Medicine, Chemistry
  • Angewandte Chemie
  • Protein folding kinetics are often measured by monitoring the change of a single spectroscopic signal, such as the fluorescence of an intrinsic fluorophore or the absorbance at a single frequency within an electronic or vibrational band of the protein backbone. While such an experimental strategy is easy to implement, the use of a single spectroscopic signal can leave important folding events undetected and overlooked. Herein, we demonstrate, using the mini-protein Trp-cage as an example, that… CONTINUE READING
    A hydrodynamic view of the first-passage folding of Trp-cage miniprotein
    5
    Infrared measurements of protein conformational dynamics

    References

    Publications referenced by this paper.
    SHOWING 1-10 OF 68 REFERENCES