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Figure 7.
Figure 7. Surface properties of the BGPh molecule and a
proposed model of its membrane bound form. (a) Arrangement of
amino acid residues on the surface are depicted as follows:
hydrophobic (white), aromatic (pink), basic (blue), acidic
(red), and polar neutral residues (green). (b) The electrostatic
potential mapped on the molecular surface; positive is in blue
and negative in red. (c) Ribbon model of the protein in the same
orientation as (a) and (b) for helping the reader to locate
these features in the structure. The active center is indicated
by arrows; the hydrophobic mound is encircled by a solid line.
The electrostatic potential map was obtained with DelPhi[42]
module of Insight II package. (d) Proposed model of BGPh bound
to the inner surface of the cell membrane. The protein molecule
is in the molecular surface model showing the calculated
electrostatic potential. The CPK model of dodecyl-  -glucoside
is placed in the active site channel of BGPh. The membrane is
modeled by an array of CPK models of glucosyl caldarchaetidic
acid and glucosyl archaeol according to De Rosa et al.[26] The
thickness of the membrane is 55 Å in the model, but it
should be thinner in live Archaea due to the disordering of core
isoprenoid chains.
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