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Maggio,B.; Rosetti,C.M.; Borioli,G.A.; Fanani,M.L.; Del Boca,M.. |
The lipids and proteins of biomembranes exhibit highly dissimilar conformations, geometrical shapes, amphipathicity, and thermodynamic properties which constrain their two-dimensional molecular packing, electrostatics, and interaction preferences. This causes inevitable development of large local tensions that frequently relax into phase or compositional immiscibility along lateral and transverse planes of the membrane. On the other hand, these effects constitute the very codes that mediate molecular and structural changes determining and controlling the possibilities for enzymatic activity, apposition and recombination in biomembranes. The presence of proteins constitutes a major perturbing factor for the membrane sculpturing both in terms of its surface... |
Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Lipid monolayers; Sphingomyelinase; C-Fos; Segregated lipid domains; Lipid-protein interaction; Anphitropic proteins. |
Ano: 2005 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005001200002 |
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