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.
Quantitative Residue-Specific Protein Backbone Torsion Angle Dynamics from Concerted Measurement of 3J Couplings
