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Monolayers of proteins: β-lactoglobulin and its interactions with phospholipids (1994)

Puggelli, M. ; Nocentini, M. ; Gabrielli, G. ; [et al.]

Springer

Il nuovo cimento della Società Italiana di Fisica 16 (1994), S. 1529-1536

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ISSN: 0392-6737

Keywords: Surface energy ; thermodynamic properties ; Conference proceedings

Source: Springer Online Journal Archives 1860-2000

Topics: Physics

Notes: Summary Monolayers of a protein β-lactoglobulin (βL) and two lipids distearoylphosphatidylcholine (DSPC) and dimirystoylphosphatidylcholine (DMPC) on aqueous subphase containing Na+ or Ca2+ ions are studied. The spreading isotherms and the ATR-FTIR spectra of LB plurilayers transferred, allow to deduce that α-helix conformation of β-lactoglobulin is the prevailing form. The study of bidimensional mixtures between βL with DSPC and with DMPC shows that the components are incompatible at the W/A interface.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF02462038

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