Abstract
Backgrounds: Enormous number of possible conformations in the protein
structure simulation have led molecular dynamics researchers to be
frustrated until now. Some methods with defects ended their experiments
into failure. This made them fail to determine the structure and
function of folded protein in stable state with the lowest potential
energy. This apparently exist in nature. The purpose of resolving a
protein folding pathway that follows protein backbone residues torsional
inertia was accomplished. Results: A new method, torsion angle modeling,
was adopted focused on the rotation of dihedral angles. The potential
energy was calculated by rotating torsion angles of the peptide with 8
residues. It was found that when moving in the order of torsional
inertia, 8 residues swivel in sequence. Six passes were repeated to find
the lowest value. Conclusion: The protein backbone torsion angle plays
very important role in predicting protein structure. Actually it was
thousand times faster or more than others to get the obvious pathway.