6533b820fe1ef96bd1279cce

RESEARCH PRODUCT

Calculation of partition coefficient and hydrophobic moment of the secondary structure of lysozyme

Francisco Torrens

subject

Models MolecularQuantitative Biology::BiomoleculesChromatographyOrganic ChemistrySolvationGeneral MedicineBiochemistryProtein Structure SecondaryAnalytical ChemistryGibbs free energyCondensed Matter::Soft Condensed MatterPartition coefficientchemistry.chemical_compoundsymbols.namesakeDipolechemistrysymbolsThermodynamicsMoleculeMuramidaseLysozymeProtein secondary structure

description

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.

yearjournalcountryeditionlanguage
2001-02-24Journal of Chromatography A
https://doi.org/10.1016/s0021-9673(00)00727-5