Use the RUN button only if the realtime display is not selected

This is a profile of the sequence in which the size of the bars is proportional to that the value of the residue's hydrophobicity index (Hi), and where hydrophobic residues (positive Hi) are in blue above the line, and hydrophilic residues (negative Hi) are in red below the line.

The mean hydrophobicity, (H) is the total hydrophobicity (sum of all residue hydrophobicity indices) divided by the number of residues.

The mean hydrophobic moment (mH) is the vectorial sum of all the hydrophobicity indices, divided by the number of residues. This depends on the conformation that has been selected, and in particular on the projection angle for successive indices on the Edmundson projection. It is shown as the green vector in the display.

The relative hydrophobic moment (mHrel) of a peptide is its hydrophobic moment relative to that of a perfectly amphipathic peptide. This gives a better idea of the amphipathicity using different scales. A value of 0.5 thus indicates that the peptide has about 50% of the maximum possible apmphipathicity. The relative hydrophobic moment is difficult to determine exactly for all cases. For the CCS scale it is calculated by creating a peptide made up only of Phe (Hi = +10) and Arg (Hi = -10), and placing them so as to obtain perfectly segregated hydrophobic/hydrophilic sectors on the Edmundson projection. For the K&D and Eidenberg scales, Ile and Arg were used. For alpha-helical peptides (projection angle = 100°), an 18 residue peptide with 9 Arg, 9 Phe/Ile was used. This results in mHmax of 6.3, 2.8 and 0.83 for the CCS, K&D and Eisenberg scales respectively. For other projections, appropriate peptide sizes corresponding to approximately one turn were used. ( NB if the sequence you are using is very short, it may have a mHrel > 1).