The effect of environment on the stability of an integral membrane helix: Molecular dynamics simulations of surfactant protein C in chloroform, methanol and water

Kovacs, H, Mark, AE, Johansson, J and Vangunsteren, WF (1995) The effect of environment on the stability of an integral membrane helix: Molecular dynamics simulations of surfactant protein C in chloroform, methanol and water. Journal of Molecular Biology, 247 4: 808-822. doi:10.1016/S0022-2836(05)80156-1


Author Kovacs, H
Mark, AE
Johansson, J
Vangunsteren, WF
Title The effect of environment on the stability of an integral membrane helix: Molecular dynamics simulations of surfactant protein C in chloroform, methanol and water
Journal name Journal of Molecular Biology   Check publisher's open access policy
ISSN 0022-2836
Publication date 1995-04-07
Sub-type Article (original research)
DOI 10.1016/S0022-2836(05)80156-1
Volume 247
Issue 4
Start page 808
End page 822
Total pages 15
Language eng
Subject 1312 Molecular Biology
2406 Virology
Abstract A series of three molecular dynamics simulations at 300 K in explicit solvent environments of chloroform, methanol and water has been performed on the pulmonary surfactant lipoprotein, SP-C, comprising several consecutive valine residues in order to investigate the stability of the α-helical conformation. Two additional simulations were performed on truncated SP-C with a five-residue N-terminal deletion at 300 K and 500 K in water, the high temperature run in order to increase the rate of peptide denaturation. Indications of destabilization appear in chloroform during 1 ns while the SP-C α-helix is remarkably stable during 1 ns in methanol and water. In particular the polyvalyl part comprising residues Val15 to Val21 remains intact even at elevated temperature, and the valines do no disrupt the α-helical conformation. The valyl-rotamer sampling is partly restricted. Unfolding takes place successively along the primary sequence starting from the C-terminal end. Factors affecting polypeptide stability in molecular dynamics simulations are addressed. The intrinsic helix-forming tendency of valine residues and its dependence on the sequence context, and the role of the solvent environment in stabilizing or destabilizing an α-helical fold, are discussed.
Keyword computer simulation
molecular dynamics
peptide conformation
solvent interactions
α-helix stability
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
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