Molecular dynamics simulations have been performed on a tetramer of the 25-residue (SSDPLVVAASIIGILHLILWILDRL) synthetic peptide which contains the transmembrane domain of the influenza A virus M2 coat protein. The peptide bundle was initially assembled as a parallel α-helix bundle in the octane portion of a phase separated water/octane system, which provided a membrane-mimetic environment. A 4-ns dynamics trajectory identified a left-handed coiled coil state of the neutral bundle, with a water filled funnel-like structural motif at the N-terminus involving the long hydrophobic sequence. The neck of the funnel begins at V27 and terminates at H37, which blocks the channel. The C-terminus is held together by inter-helix hydrogen bonds and contains water below H37. Solvation of the S23 and D24 residues, located at the rim of the funnel, appears to be important for stability of the structure. The calculated average tilt of the helices in the neutral bundle is 27±5°, which agrees well with recent NMR data. Copyright (C) 1998 Federation of European Biochemical Societies.
Zhong, Q., Husslein, T., Moore, P. B., Newns, D. M., Pattnaik, P., & Klein, M. L. (1998). The M2 channel of influenza A virus: A molecular dynamics study. FEBS Letters, 434(3), 265–271. https://doi.org/10.1016/S0014-5793(98)00988-0