|Title||Conformation and aggregation of M13 coat protein studied by molecular dynamics.|
|Publication Type||Journal Article|
|Year of Publication||1991|
|Authors||Sanders, J. C., N. A. J. van Nuland, O. Edholm, and M. A. Hemminga|
|Date Published||1991 Nov|
|Keywords||Amino Acid Sequence, Capsid, Capsid Proteins, Membrane Proteins, Molecular Sequence Data, Protein Conformation|
Molecular dynamics (MD) simulations are performed on M13 coat protein, a small membrane protein for which both alpha- and beta-structures have been suggested. The simulations are started from initial conformations that are either monomers or dimers of alpha-helices or U-shaped beta-sheets. The lipid bilayer is represented by a hydrophobic potential. The results are analyzed in terms of stability, energy and secondary structure. The U-shaped beta-structure changes from a planar to a twisted form with larger twist for the monomer than the dimer. The beta-sheet is much more flexible than the alpha-helix as monitored by the root mean square (rms) fluctuations of the C alpha atoms. A comparison of the energies after 100 ps MD simulation shows that of the monomers, the alpha-helix has the lowest energy. The energy difference between alpha- and beta-structures decreases from 266 kJ/mol to 148 kJ/mol, when going from monomers to dimers. It is expected that this difference will decrease with higher aggregation numbers.
|Alternate Journal||Biophys. Chem.|