Calculation of partition coefficient and hydrophobic moment of the secondary structure of lysozyme.
A method that permits a semiquantitative estimate of the partitioning of any solute between any two media is presented. As an example, the partition coefficients and hydrophobic moment of the secondary structure of lysozyme are calculated. Program GSCAP is written as a version of Pascal's solvent-dependent conformational analysis (SCAP) program. The dipole moments calculated for the helices are trebled with respect to that for the sheet. For helices, the main contribution to the water-accessible surface area is the hydrophobic term, while the hydrophilic part dominates in the sheet. Molecular globularity and the three studied partition coefficients differentiate between helices and sheet.
Torrens
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Departament de Quimíca Física, Facultat de Química, Universitat de València, Spain. francisco.torrens@uv.es
D008958:Models, Molecular; D009113:Muramidase / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013816:Thermodynamics
D009113:Muramidase