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Figure 3.
Figure 3. The structure of the 29–103 region of p112. (a)
Superposition of the main-chains of 20 refined structures for
the residues 29–103. N and C indicate K29 and A103,
respectively, and loop 3 is labeled. (b) Schematic drawing of
the restrained energy minimized mean structure derived from the
20 refined structures for 29–103, as viewed from the same
direction as in (a). (c) Hydrophobic core. Overlaying of the 20
structures of the side-chains for residues involved in the
hydrophobic core is shown on the main-chain of the restrained
energy minimized mean structure. The α-helices and β-strands
are colored in red and blue, respectively. (d) Hydrophobic patch
exposed to the solvent. The same overlaying as in (c) is shown
for F31, F71 and F73, being rotated by ca. 90 ° from (c).
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