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Provedor de dados:  BJMBR
País:  Brazil
Título:  Protein-mediated surface structuring in biomembranes
Autores:  Maggio,B.
Rosetti,C.M.
Borioli,G.A.
Fanani,M.L.
Del Boca,M.
Data:  2005-12-01
Ano:  2005
Palavras-chave:  Lipid monolayers
Sphingomyelinase
C-Fos
Segregated lipid domains
Lipid-protein interaction
Anphitropic proteins
Resumo:  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 topography and dynamics. We will focus on some results from our group within this context and summarize some recent evidence for the active involvement of extrinsic (myelin basic protein), integral (Folch-Lees proteolipid protein) and amphitropic (c-Fos and c-Jun) proteins, as well as a membrane-active amphitropic phosphohydrolytic enzyme (neutral sphingomyelinase), in the process of lateral segregation and dynamics of phase domains, sculpturing of the surface topography, and the bi-directional modulation of the membrane biochemical reactivity.
Tipo:  Info:eu-repo/semantics/article
Idioma:  Inglês
Identificador:  http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005001200002
Editor:  Associação Brasileira de Divulgação Científica
Relação:  10.1590/S0100-879X2005001200002
Formato:  text/html
Fonte:  Brazilian Journal of Medical and Biological Research v.38 n.12 2005
Direitos:  info:eu-repo/semantics/openAccess
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