@article {Sanchez-Hidalgo:2010:0929-8665:708,
title = "Conformational Stability and Activity of Circular Enterocin AS-48 Derivatives",
journal = "Protein and Peptide Letters",
parent_itemid = "infobike://ben/ppl",
publishercode ="ben",
year = "2010",
volume = "17",
number = "6",
publication date ="2010-06-01T00:00:00",
pages = "708-714",
itemtype = "ARTICLE",
issn = "0929-8665",
url = "https://www.ingentaconnect.com/content/ben/ppl/2010/00000017/00000006/art00004",
doi = "doi:10.2174/092986610791190390",
keyword = "Circular antimicrobial peptides, lactic-acid bacteria, enterococci, site-directed mutagenesis",
author = "Sanchez-Hidalgo, Marina and M Fernandez-Escamilla, Ana and Martinez-Bueno, Manuel and Valdivia, Eva and Serrano, Luis and Maqueda, Mercedes",
abstract = "Four AS-48 mutants (Trp24Ala, Gly13Lys, Leu40Lys and Ala53Ser) were obtained by site-directed mutagenesis. The minimal inhibitory concentration of each peptide showed that only residue Trp24 was unquestionably involved in the biological activity. Guanidine hydrochloride-induced unfolding assays showed a three-state transition denaturation process, suggesting a molten-globule-like conformation after the first transition. ",
}