@article{bibcite_158,
  keywords = {Models, Molecular, Peptides, Protein Folding, Protein Structure, Secondary, Monte Carlo Method, Proteins, Models, Theoretical, Models, Statistical, Time Factors, Biophysics, Chemistry, Physical, Cluster Analysis, Probability},
  author = {F. Rao and G. Settanni and E. Guarnera and A. Caflisch},
  title = {Estimation of protein folding probability from equilibrium simulations},
  abstract = {<p>The assumption that similar structures have similar folding probabilities (p<sub>fold</sub>) leads naturally to a procedure to evaluate p<sub>fold</sub> for every snapshot saved along an equilibrium folding-unfolding trajectory of a structured peptide or protein. The procedure utilizes a structurally homogeneous clustering and does not require any additional simulation. It can be used to detect multiple folding pathways as shown for a three-stranded antiparallel \&beta;-sheet peptide investigated by implicit solvent molecular dynamics simulations.</p>},
  year = {2005},
  journal = {Journal of Chemical Physics},
  volume = {122},
  pages = {184901},
  month = {2005 May 8},
  issn = {0021-9606},
  doi = {10.1063/1.1893753},
  language = {eng},
}