Property Calculation allows calculating the following physicochemical properties of peptides: Normalized Hydrophobic Moment, Normalized Hydrophobicity, Net Charge, Isoelectric Point, Penetration Depth, Tilt Angle, Propensity to Disordering, Linear Moment, Propensity to in vitro Aggregation, Angle Subtended by the Hydrophobic Residues, Amphiphilicity Index, and Propensity to ppII coil. The following properties: Normalized Hydrophobic Moment, Normalized Hydrophobicity, Linear Moment, and Angle Subtended by the Hydrophobic Residues can be calculated for different hydrophobic scales selected from the drop-down menu. The following hydrophobic scales are available: MF – Moon and Fleming scale (Moon, C. P.; Fleming, Proc. Natl. Acad. Sci. U. S. A. 2011, 108 (25), 10174-10177), KD – Kyte and Doolittle scale (Kyte J., Doolittle R. F. J. Mol. Biol. 1982, 157 (1), 105-132.), WW – Wimley and White scale (Wimley W. C., White S. H. Nat. Struct. Biol. 1996, 3, 842-848.), EW – Eisenberg and Weiss (Eisenberg D. at all Proc. Natl. Acad. Sci. U. S. A. 1984, 81 (1), 140-144.), UH – Unified Hydrophobic scale (Koehler J. at all Proteins 2009, 76, 13-29.) HW – Hessa and White scale (Hessa, T at all Nature 2005, 433, 377-381.). Values of the properties given in the Peptide Cards have been calculated for the KD scale.
Paste sequence(s) in FASTA format (the peptide sequence can contain the '+' sign to the end in case of C-terminal amidation):
Note: Sequence(s) should consist of 20 canonical amino acids.