Using a solvent-referenced energy calculation, a 16-residue peptide with alanine side chains folded into predominantly alpha-helical conformations during constant temperature (274 K) simulations. From different initial conformations, helical conformations were reached and the multiple energy minima did not become a serious problem. Under the same conditions, the simulation did not indiscriminately fold a sequence such as polyglycine into stable helices. Interesting observations from the simulations relate to the folding mechanism. The electrostatic interactions between the successive amides favored extended conformations (or beta strands) and caused energy barriers to helix folding. beta-bends were observed as intermediates during helix nucleation. The helix propagation toward the C-terminus seemed faster than that toward the N-terminus. In helical conformations, hydrogen bond oscillation between the i,i+ 4 and the i,i+3 patterns was observed. The i,i+3 hydrogen bonds occurred more frequently during helix propagation and deformation near both ends of the helical segment.
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