Database of Antimicrobial Activity and Structure of Peptides
Count of Peptides :

Composition of Database according to Type of Synthesis of monomeric peptides

Composition of Database according to Complexity of peptides

Distribution of lengths of sequences for all peptides

Distribution of lengths of sequences for ribosomal peptides

Composition of Database according to Taxa (Kingdom) of Source Organism

Composition of Database according to Target Groups

Amino acid composition of Ribosomal monomeric peptides

Positivly Charged Negativly Charged Hydrophobic Small Polar Uncharged Unsual

Amino acid composition of Synthetic monomeric peptides

Positivly Charged Negativly Charged Hydrophobic Small Polar Uncharged Unsual

Amino acid composition of Ribosomal monomeric peptides relative to UniProt

Positivly Charged Negativly Charged Hydrophobic Small Polar Uncharged Unsual

Amino acid composition of Synthetic monomeric peptides relative to UniProt

Positivly Charged Negativly Charged Hydrophobic Small Polar Uncharged Unsual

Statistics of occurrence of sequential pairs of positively charged amino acids (Lys, Arg) with i residues between them ( I = 0,1,2,…,14) in the ribosomal peptides.

Fi+ 3σi fi Fi- 3σi
Statistics has presented by observed frequencies fi ( relied on the DBAASP data) expected frequencies Fi and their standard deviation σi ( estimated on the base of randomly generated sequences). i is a number of residues between positively charged residues (R,K).

The statistics of occurrence of sequential pairs of Cysteines (Cys) with I residues (i=1,2,…,10) between them in the ribosomal peptides.

Fi+ 3σi fi Fi- 3σi
Statistics has presented by observed frequencies fi ( relied on the DBAASP data) expected frequencies Fi and their standard deviation σi ( estimated on the base of randomly generated sequences). i is a number of residues between sequential pairs of Cysteines (C).

The statistics of occurrence of sequential pairs of small amino acids (Gly,Ala) with I residues (i=1,2,…,10) between them in the ribosomal peptides.

Fi+ 3σi fi Fi- 3σi
Statistics has presented by observed frequencies fi ( relied on the DBAASP data) expected frequencies Fi and their standard deviation σi ( estimated on the base of randomly generated sequences). i is a number of residues between sequential pairs of small amino acids (A,G).

The statistics of occurrence of sequential pairs of hydrophobic beta-branched amino acids (Ile,Val,Phe) with I residues (i=1,2,…,10) between them in the ribosomal peptides.

Fi+ 3σi fi Fi- 3σi
Statistics has presented by observed frequencies fi ( relied on the DBAASP data) expected frequencies Fi and their standard deviation σi ( estimated on the base of randomly generated sequences). i is a number of residues between sequential pairs of hydrophobic beta-branched amino acids (I,V,F).

Distribution of Normalized Hydrophobicities of peptides

Distribution of Normalized Hydrophobic Moments of peptides

Distribution of Charges of peptides

Distribution of Isoelectric Points of peptides

Distribution of Depths of Penetration in the membrane of peptides

Distribution of Tilt Angles of peptides relative to membrane surface

Distribution of Propensities to Disordering of peptides

Distribution of Linear moments of peptides

Distribution of Propensities to in vitro Aggregation of peptides