Adsorption of platinum on the stoichiometric RuO2(110) surface
Density functional theory was used to calculate the geometries and electronic structures of Pt adsorption on the stoichiometric RuO2(110) surface at different coverages. The calculated results reveale...
Density functional theory was used to calculate the geometries and electronic structures of Pt adsorption on the stoichiometric RuO2(110) surface at different coverages. The calculated results reveale...
Optimized effective potentials yielding Hartree–Fock energies and densities
It is commonly believed that the exchange-only optimized effective potential (OEP) method must yield total energies that are above corresponding ground-state Hartree–Fock (HF) energies except for...
It is commonly believed that the exchange-only optimized effective potential (OEP) method must yield total energies that are above corresponding ground-state Hartree–Fock (HF) energies except for...
Absence of reptation in the high-temperature folding of the trpzip2 
-hairpin peptide
J. Chem. Phys. 124, 141102 (2006); doi:10.1063/1.2190226
Published 14 April 2006
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We have carried out extensive all atom explicit solvent simulations of the high-temperature folding and unfolding of the trpzip2 -hairpin peptide and examined the resulting trajectories for evidence of folding via a reptation mechanism. Over 300 microcanonical simulations of 10 ns each were initiated from a Boltzmann ensemble of conformations at 425 K. Though we observed numerous folding and unfolding events, no evidence of reptation was found. The diffusional dynamics of the peptide are orders of magnitude faster than any observed reptation-like motion. Our data suggest that the dominant mechanisms for -hairpin folding under these conditions are hydrophobic collapse and turn formation, and that rearrangements occur via significant expansion of the polypeptide chain.
©2006 American Institute of Physics
-hairpin peptide and examined the resulting trajectories for evidence of folding via a reptation mechanism. Over 300 microcanonical simulations of 10 ns each were initiated from a Boltzmann ensemble of conformations at 425 K. Though we observed numerous folding and unfolding events, no evidence of reptation was found. The diffusional dynamics of the peptide are orders of magnitude faster than any observed reptation-like motion. Our data suggest that the dominant mechanisms for -hairpin folding under these conditions are hydrophobic collapse and turn formation, and that rearrangements occur via significant expansion of the polypeptide chain.
©2006 American Institute of Physics
| History: | Received 7 February 2006; accepted 3 March 2006; published 14 April 2006 |
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http://link.aip.org/link/?JCPSA6/124/141102/1 |
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1089-7690 (online)
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REFERENCES (23)
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