Moricin is a antibacterial peptide that is highly basic. The structure of moricin reveals that it is comprised of a long alpha-helix. The N terminus of the helix is amphipathic, and the C terminus of the helix is predominately hydrophobic. The amphipathic N-terminal segment of the alpha- helix is mainly responsible for the increase in permeability of the bacterial membrane which kills the bacteria [PMID: 11997013].
Note:
The format for Signature ID is the family name, followed by H or P for HMM or Pattern respectively. The integer suffixed to H or P denotes the length of the sequences used to create the family signature. If no integer is suffixed, it indicates that the signature was created using all the sequences of the family. The integer following the underscore denotes the number of sequences used for the creation of signatures.
For example:
AureinH_21 is a HMM for Aurein family created using 21 sequences.
AureinP16_9 is a pattern for Aurein family derived using 9 input sequences that are 16 residues long.
