Publication Abstract from PubMed
Bridge not required: The disulfide bridge in the antibacterial peptide leucocin A was replaced with two Ser or two Leu residues. The double leucine mutant was found to be active, and elucidation of its 3D structure showed that the two leucines interact to hold the N- and C-terminal domains together.
Substitution of a Conserved Disulfide in the Type IIa Bacteriocin, Leucocin A, with L-Leucine and L-Serine Residues: Effects on Activity and Three-Dimensional Structure.,Sit CS, Lohans CT, van Belkum MJ, Campbell CD, Miskolzie M, Vederas JC Chembiochem. 2012 Jan 2;13(1):35-8. doi: 10.1002/cbic.201100634. Epub 2011, Nov 25. PMID:22121114[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
