A Monte Carlo model of fd and Pf1 coat proteins in lipid membranes.
A Monte Carlo Dynamics simulation was used to investigate the behavior of filamentous bacteriophage coat proteins in a model membrane environment. Our simulation agrees with the previous experimental observations that despite the low sequence similarity between the major coat proteins of Pf1 and fd bacteriophages, their structure in the membrane environment is very similar. These results support the hypothesis that the hydrophobic effect exerts an important influence on membrane protein structure. The model may also be used for modeling the insertion and transport processes in protein-membrane systems. The example of fd protein was also used as a test of sensitivity of our model to temperature, thickness of the hydrocarbon phase, and simulation time. In all cases, the results were independent (over the tested range) of the particular values of the parameters.
Milik
M
M
Scripps Research Institute, Department of Molecular Biology, La Jolla, California 92037, USA.
Skolnick
J
J
D000595:Amino Acid Sequence; D002213:Capsid / Q000737:chemistry*; D017912:Inovirus / Q000737:chemistry*; D008081:Liposomes; D008961:Models, Structural; D008962:Models, Theoretical; D008969:Molecular Sequence Data; D009010:Monte Carlo Method; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid
D008081:Liposomes