General Data Compositional DataNEW Physical, Chemical Data

Physicochemical features of AMP , such as hydrophobicity, charge, amphipathicity, predisposition to interaction with cell envelope and so on, determine the mode of action. Physicochemical features are determined by amino acid sequences, for example, by amino acid compositions and distribution of particular amino acids along the chain. Mode of action determined by amino acid compositions and distributions can be different. So, it's interesting to know differences in amino acid compositions and distributions along the chain between different groups of AMPs, for example: between linear and non-linear; between long ( > 25 aa) and short ( < 15 aa); between AMPs that are active against different species; etc . Current tool relying on DBAASP data allows to perform such assessments for sequences consisting of not modified amino acids. The parameter "Minimal Peptide count" means a threshold for which statistics will not be assessed. User can choose convenient value of threshold. The default value equals 100;









Positively Charged Negatively Charged Hydrophobic Small Polar Uncharged Unusual








Positively Charged Negatively Charged Hydrophobic Small Polar Uncharged Unusual

X can be selected from dropdown menus and will present a particular amino acid (for example A or G or R etc) or group of amino acids (for example hydrophobic (L,I,V,F,A,W) or charged (R, K, E, D) or any group desired)


Statistics has presented by observed frequencies fi ( relied on the DBAASP data), average value of expected frequencies Fi and their standard deviation σi (i=0,1,2,...,10). Expected frequencies are estimated for random sequences generated by random shuffling of sequences of considered set of peptides. Shuffling is repeated 500 times to assess average and standard deviation.














Fi+ 3σi fi Fi- 3σi
Distribution of () residues

X and Y are a particular amino acids and can be selected from dropdown menus. The statistics built for XY pair is distinguished from statistics built for YX pair. The X is chosen from first (left) menu and Y from right corresponds to XY pairs and vise versa

Statistics has presented by observed frequencies fi ( relied on the DBAASP data), average value of expected frequencies Fi and their standard deviation σi (i=0,1,2,...,10). Expected frequencies are estimated for random sequences generated by random shuffling of sequences of considered set of peptides. Shuffling is repeated 500 times to assess average and standard deviation.














Fi+ 3σi fi Fi- 3σi
Distribution of () residues