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Figure 2.
Fig. 2. Isolated core alanines create holes in the coiled
coil. Shown is a series of space-filling models of consecutive
stretches of the structure, each one viewing the broad face of
the coiled coil. The region from residue 141 to the C terminus
of the fragment is well packed [average gap volume = 30 Å3
per residue pair (see Table 4, which is published as supporting
information on the PNAS web site)] whereas that from residues
113-141 contains significant holes in the core (average gap
volume = 67 Å3 per residue pair). The quality of the
packing between the helices of the coiled coil relates to the
sequential pattern of the sizes of the side chains at the
interface between the helices (see Results and letters in Fig.
3).
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