Microfolding: conformational probability map for the alanine dipeptide in water from molecular dynamics simulations
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Updated: Oct 23, 2026
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Published on: April 10, 2012
1Department of Biochemistry, School of Medicine, University of North Carolina, Chapel Hill 27599-7260.
Proteins
|January 1, 1988
Abstract:
A direct attack on the protein-folding problem has been initiated with the free energy perturbation methods of molecular dynamics. The complete conformational probability map for the alanine dipeptide is presented. This work uses the SPC model for the explicit hydration of the dipeptide. Free energy differences for the four observed minima (beta, alpha R, alpha L, C7ax) are given, and the free energy barriers between minima are outlined.
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