The assingnment of secondary structure to either loop, helix or strand
was performed by combining the prediction profiles shown in Figure 1
with an analysis of conservation patterns. The strands and helices
described in the previous sections show reasonable consistency for one
predicted state. However, three regions do not show such consistency
and are therefore difficult to assign either to - or
-
conformation. The region 118-128 starts with a cluster of conserved
hydrophobic residues (118-124) indicative of a buried
- strand, this
is continued by an alternating hydrophobic/hydrophilic pattern
suggesting that the buried
- strand may extend into a surface strand
(125-127). The loop 128-131 conserves proline at 129 and the
following region is predicted
- (132-135). Type II (proline) turns
often occur between consecutive antiparallel
- strands, so the
conservation of proline lends support to the prediction of
-
structure on either side of the 132-135 loop. However, this conflicts
with the prediction profiles that suggest this region is an
- helix.
At 144-150 the prediction profiles suggest - strand, but conserved
hydrophobics at 144, 147, 148 and 150 indicate a surface
- helix.
The tolerance of Gly at 146 may swing the prediction in favour of
-
rather than
- structure.
The variable sequence composition at 330-C-terminus make the region
difficult to assign to - or
-. The region might be split into two
- strands (333-339, 347-353), or possibly a single helix if the gap
at 342-344 is closed.