@article {Seidler:2009:0929-8665:182,
title = "Interfacial Effects on the Conformation of Amyloid-Beta Peptide",
journal = "Protein and Peptide Letters",
parent_itemid = "infobike://ben/ppl",
publishercode ="ben",
year = "2009",
volume = "16",
number = "2",
publication date ="2009-02-01T00:00:00",
pages = "182-188",
itemtype = "ARTICLE",
issn = "0929-8665",
url = "https://www.ingentaconnect.com/content/ben/ppl/2009/00000016/00000002/art00012",
doi = "doi:10.2174/092986609787316324",
keyword = "fluorescence, Amyloid-beta, protein folding, interface, sevoflurane",
author = "Seidler, Norbert W. and Eklund, Joshua D.",
abstract = "We examined the effects of air-water and water-sevoflurane interfaces on conformational properties of amyloid- peptide (ABP). Fractions were extracted from sub-interfacial (air-water) and supra-interfacial (water-sevoflurane) layers and compared with aqueous bulk layers using fluorescence properties of ABP provided by a single tyrosine. The observations suggest that interfacial ABP may be more disordered than bulk ABP. ",
}