Molecular Dynamics of Pf1 Coat Protein in a Phospholipid Bilayer

  • Benoît Roux
  • Thomas B. Woolf


The anchoring, stabilization, and function of membrane proteins is of central importance for understanding numerous fundamental biological processes occurring at the surface of the cell. In recent years, extensive efforts have been devoted to develop such powerful tools as X-ray crystallography (Deisenhofer and Michel, 1989; Cowan et al, 1992; Weiss and Schulz, 1992; Picot et al, 1994), electron microscopy (Henderson et al, 1990) and nuclear magnetic resonance (Cross and Opella, 1994) to determine the three-dimensional structure of membrane proteins. Despite this progress, many of the factors responsible for the function of biomembranes are still poorly understood. This is due, in large part, to the extreme difficulties in applying experimental methods to obtain detailed information about the phospholipid bilayer environment and its influence on the structure, dynamics, and function of membrane proteins. In a simplified view, the membrane-solution interface is often pictured as a relatively sharp demarcation between the hydrophilic and hydrophobic regions (Edholm and Jahnig, 1988; Milik and Skolnick, 1993). Its dominant effect is usually represented as that of a thermodynamic driving force partitioning the amino acids according to their solubility (Eisenberg et al, 1982; Engelman et al, 1986; Wesson and Eisenberg, 1992); hydrophobic amino acids are more likely to be found within the hydrocarbon core of the membrane, whereas charged and polar amino acids are more likely to be found in the bulk solvent.


Molecular Dynamic Simulation Coat Protein Phospholipid Bilayer Amphipathic Helix DPPC Bilayer 
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© Birkhäuser Boston 1996

Authors and Affiliations

  • Benoît Roux
  • Thomas B. Woolf

There are no affiliations available

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