Author | Conference | Journal | Organization | Year | DOI
Look for results that meet for the following criteria:
Academic
Publications
How Robust Are Protein Folding Simulations with Respect to Force Field Parameterization?

How Robust Are Protein Folding Simulations with Respect to Force Field Parameterization?,10.1016/j.bpj.2011.03.051,Biophysical Journal,Stefano Piana,K

Edit
How Robust Are Protein Folding Simulations with Respect to Force Field Parameterization?   (Citations: 4)
BibTex | RIS | RefWorks Download
Molecular dynamics simulations hold the promise of providing an atomic-level description of protein folding that cannot easily be obtained from experiments. Here, we examine the extent to which the molecular mechanics force field used in such simulations might influence the observed folding pathways. To that end, we performed equilibrium simulations of a fast-folding variant of the villin headpiece using four different force fields. In each simulation, we observed a large number of transitions between the unfolded and folded states, and in all four cases, both the rate of folding and the structure of the native state were in good agreement with experiments. We found, however, that the folding mechanism and the properties of the unfolded state depend substantially on the choice of force field. We thus conclude that although it is important to match a single, experimentally determined structure and folding rate, this does not ensure that a given simulation will provide a unique and correct description of the full free-energy surface and the mechanism of folding.
Journal: Biophysical Journal - BIOPHYS J , vol. 100, no. 9, pp. L47-L49, 2011
Cumulative Annual
View Publication
The following links allow you to view full publications. These links are maintained by other sources not affiliated with Microsoft Academic Search.
Sort by:

Citations (4)

Share this on