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Figure 8.
Figure 8 Prediction of a myomesin filament beads-on-the-string
model, consisting of 2  5
Ig domains that are connected by  -helical
linkers and end-to-end C-terminal assembly. (A)
Beads-on-the-string presentation of the crystal structure of the
My12–My13 dimeric assembly of the myomesin C-terminus (cp.
Figure 1). (B) Schematic model of the My9–My13 C-terminal
filament, in which adjacent domains are connected by -helical
linkers. (C) Prediction of -helical
segments at repetitive sequence intervals, interspersed myomesin
domains My9, My10, My11, My12 and My13, using PredictProtein
(Rost et al, 2004). The starting residue number, the sequence
interval with respect to the previous predicted -helical
segment and the sequence of each predicted -helix
segment are presented. Residues that are predicted to be -helical
by PROF (for details, see PredictProtein) are shown in capital
characters, and those that are predicted with a confidence level
of at least 82% are shown by small characters. The predicted
helix length, using the two categories, is indicated (second
number in parentheses). For comparison, the experimentally
determined My12–My13-connecting helix is highlighted in green.
(D) Circular dichroism curves of My12–My13 (blue) and
My9–My13 (magenta). The estimates for secondary structural
elements for My12–My13 and My9–My13 are as follows: helix,
0.23/0.19; strand, 0.26/0.36; turn, 0.18/0.13; unordered,
0.33/0.34.
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