Isabella Daidone

Summary

Affiliation: University of Heidelberg
Country: Germany

Publications

  1. pmc Hydrogen-bond driven loop-closure kinetics in unfolded polypeptide chains
    Isabella Daidone
    Interdisciplinary Center for Scientific Computing, University of Heidelberg, Heidelberg, Germany
    PLoS Comput Biol 6:e1000645. 2010
  2. pmc Structured pathway across the transition state for peptide folding revealed by molecular dynamics simulations
    Lipi Thukral
    Interdisciplinary Center for Scientific Computing, University of Heidelberg, Heidelberg, Germany
    PLoS Comput Biol 7:e1002137. 2011
  3. pmc Dehydration-driven solvent exposure of hydrophobic surfaces as a driving force in peptide folding
    Isabella Daidone
    Interdisciplinary Center for Scientific Computing, University of Heidelberg, Im Neuenheimer Feld 368, 69120 Heidelberg, Germany
    Proc Natl Acad Sci U S A 104:15230-5. 2007
  4. ncbi request reprint Subdiffusion in peptides originates from the fractal-like structure of configuration space
    Thomas Neusius
    Computational Molecular Biophysics, Interdisziplinäres Zentrum für wissenschaftliches Rechnen IWR, Universitat Heidelberg, Im Neuenheimer Feld 368, D 69120 Heidelberg, Germany
    Phys Rev Lett 100:188103. 2008
  5. doi request reprint Common folding mechanism of a beta-hairpin peptide via non-native turn formation revealed by unbiased molecular dynamics simulations
    Lipi Thukral
    Interdisciplinary Center for Scientific Computing, University of Heidelberg, Im Neuenheimer Feld 368, 69120 Heidelberg, Germany
    J Am Chem Soc 131:18147-52. 2009
  6. doi request reprint Mechanism of DNA recognition by the restriction enzyme EcoRV
    Mai Zahran
    Computational Molecular Biophysics, IWR, University of Heidelberg, 69120 Heidelberg, Germany
    J Mol Biol 401:415-32. 2010

Detail Information

Publications6

  1. pmc Hydrogen-bond driven loop-closure kinetics in unfolded polypeptide chains
    Isabella Daidone
    Interdisciplinary Center for Scientific Computing, University of Heidelberg, Heidelberg, Germany
    PLoS Comput Biol 6:e1000645. 2010
    ....
  2. pmc Structured pathway across the transition state for peptide folding revealed by molecular dynamics simulations
    Lipi Thukral
    Interdisciplinary Center for Scientific Computing, University of Heidelberg, Heidelberg, Germany
    PLoS Comput Biol 7:e1002137. 2011
    ..The present results indicate a directed stepwise process to folding the peptide...
  3. pmc Dehydration-driven solvent exposure of hydrophobic surfaces as a driving force in peptide folding
    Isabella Daidone
    Interdisciplinary Center for Scientific Computing, University of Heidelberg, Im Neuenheimer Feld 368, 69120 Heidelberg, Germany
    Proc Natl Acad Sci U S A 104:15230-5. 2007
    ..The results suggest that dehydration-driven solvent exposure of hydrophobic surfaces may be a significant factor determining peptide conformational equilibria...
  4. ncbi request reprint Subdiffusion in peptides originates from the fractal-like structure of configuration space
    Thomas Neusius
    Computational Molecular Biophysics, Interdisziplinäres Zentrum für wissenschaftliches Rechnen IWR, Universitat Heidelberg, Im Neuenheimer Feld 368, D 69120 Heidelberg, Germany
    Phys Rev Lett 100:188103. 2008
    ..Trap models, involving a random walk with a distribution of waiting times, cannot account for the subdiffusion, which is found rather to arise from the fractal-like structure of the accessible configuration space...
  5. doi request reprint Common folding mechanism of a beta-hairpin peptide via non-native turn formation revealed by unbiased molecular dynamics simulations
    Lipi Thukral
    Interdisciplinary Center for Scientific Computing, University of Heidelberg, Im Neuenheimer Feld 368, 69120 Heidelberg, Germany
    J Am Chem Soc 131:18147-52. 2009
    ..Instead, the peptide is always observed to form partially structured conformations involving a non-native (ESYI) turn from which the native (NPDG) turn forms, triggering the folding to the beta-hairpin...
  6. doi request reprint Mechanism of DNA recognition by the restriction enzyme EcoRV
    Mai Zahran
    Computational Molecular Biophysics, IWR, University of Heidelberg, 69120 Heidelberg, Germany
    J Mol Biol 401:415-32. 2010
    ..In the third step, the flexibility of the center base pair is probed, and in the case of the full cognate sequence the DNA bends, the complex strengthens and the protein and DNA interact more closely, allowing cleavage...