A mean of 81 % of the welldetermined helices are present in the comparative structure.
In the latter cases, the coupling efficiency will depend on the nature of the interactions between helices.
The peptides are 20 and 23 residues long respectively and are predicted to form amphipathic helices.
The inner wall of the complex is formed by the 9 a-apoprotein helices.
Thus, fusion between double helices can occur between strands of the same polarity or of opposite polarity.
Sensor domains were identified as the segment between predicted transmembrane helices associated with histidine kinase domains.
In this model, the amphipathic peptide helices associate to form a bundle, which resembles a barrel composed of helices as staves.
Isolated base pairs are usually unstable ; hence, helices usually consist of at least two pairs.
