Effect of pressure on the self-association of melittin.
The effect of increased hydrostatic pressure (1 bar to 1.8 kbar) on the self-association of melittin was measured by using the fluorescence anisotropy of its single tryptophan residue. The degree of self-association was found to decrease with increasing pressure. The volume change (delta V) for dissociation is surprisingly large. At low pressures, delta V for dissociation is near -150 mL/mol. The magnitude of the volume change decreased with increasing pressure, possibly as a result of pressure-induced compression of free volume trapped at the subunit interface region of the tetramer. Overall, the pressure-dependent association of melittin is comparable to that expected for hydrophobic interactions and to that found for micelle formation by detergents.
D001514:Bee Venoms / Q000378:metabolism*; D005454:Fluorescence Polarization; D046911:Macromolecular Substances; D008433:Mathematics; D008555:Melitten / Q000378:metabolism*; D011312:Pressure; D011487:Protein Conformation; D013816:Thermodynamics; D014364:Tryptophan
D001514:Bee Venoms; D046911:Macromolecular Substances; D008555:Melitten; D014364:Tryptophan