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J. Biol. Chem., Vol. 266, Issue 24, 16120-16127, 08, 1991
R Brasseur
Several types of lipid-associating helices exist: transmembrane helices
such as in receptor proteins, pore-forming helices in ion channel proteins,
fusion-inducing peptides in viral proteins, and amphipathic helices such as
in plasma apolipoproteins. In order to propose a classification of these
helices according to their molecular properties, we introduce the concept
of molecular hydrophobicity potential for such helical segments. The
calculation of this parameter for alpha-helices enables the visualization
of the hydrophobic and hydrophilic envelopes around the peptide and their
three-dimensional representation by molecular graphics. We have used this
parameter to differentiate between pore-forming helices with a hydrophobic
envelope larger than the hydrophilic component, membrane-spanning helices
surrounded almost entirely by an hydrophobic envelope, fusiogenic peptides
with an hydrophobicity gradient both around the helix and along the axis,
and finally, amphipathic helices with a predominantly hydrophilic envelope.
The structure of the lipid-protein complexes is determined by a number of
different interactions: the hydrophobic interaction of the apolar faces of
the helices with lipids, the polar interaction of the hydrophilic sides of
different helices with each other, and the interaction of hydrophilic
residues with the aqueous solvent. The relative magnitude of the
hydrophobic and hydrophilic envelopes accounts for the differences in the
structure of the lipid- protein complexes. Purely hydrophobic interactions
stabilize transmembrane helical segments, while hydrophobic interactions
with the lipid phase and with each other are involved in the stabilization
of the pore-forming helices. In contrast, both hydrophobic interactions
with the lipids and hydrophilic interactions with the aqueous phase
contribute to the arrangement of amphipathic helices around the edges of
the discoidal lipid-apoprotein complexes.
Differentiation of lipid-associating helices by use of three- dimensional molecular hydrophobicity potential calculations
Laboratoire Chimie Physique des Macromolecules aux Interfaces CP 206-2, Universite Libre de Bruxelles, Belgium.
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