Suchergebnisse

Segregation of hydrophobic and hydrophilic domains is central to the formation of biological membranes, lipid bilayers and micelles and is also involved in protein folding. In this paper we introduce a new empirical equation which enables the calculation of the free energy of solvatation for all protein constituents.
The free energy of solvatation consists of two components ; the first derives from interactions between the constituent atoms of the protein, while the second results from interactions between protein and solvent, as expressed by the surface area of protein atoms covered by solvent molecules. The total energy of the macromolecular system is distributed along the torsional axes of the protein.
We propose here that protein folding can be represented as the aggregate of two computational procedures. The first step calculates the initial structure subsequently used in the molecular dynamics approach. For this purpose a local minimum energy procedure defines the most stable secondary structure of each amino acid which occurs during the theoretical conformational transition of the protein from an ideal alpha-helix to an ideal beta-sheet. The second calculation procedure consists of a molecular dynamics approach applied to the torsional axes of the protein, to identify the structure of the protein with a minimal total energy. This " ab initio " method therefore requires no