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 Arnaldo L. Serrano and Michelle R Bunagan and Feng Gai},
  journal={Angewandte Chemie},
  year={2011},
  volume={50 46},
  pages={10884-7}
}
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 miniprotein Trp-cage as an example, that… CONTINUE READING