Interaction of prostatic acid phosphatase fragments with a lipid bilayer as studied by NMR spectroscopy

dc.contributor.author	Filippov A.
dc.contributor.author	Khakimov A.
dc.contributor.author	Afonin S.
dc.contributor.author	Antzutkin O.
dc.date.accessioned	2018-09-18T20:11:40Z
dc.date.available	2018-09-18T20:11:40Z
dc.date.issued	2013
dc.identifier.issn	0959-9436
dc.identifier.uri	https://dspace.kpfu.ru/xmlui/handle/net/137451
dc.description.abstract	The effects of five fragments of prostatic acid phosphatase on dimyristoylphosphatidylcholine lipid multi-lamellar liposomes were studied by 2H and 31P NMR spectroscopy and those on planar supported multi-bilayers of the same lipid, by 1H and 31P NMR spectro-scopy. It was found that hydrophobic interaction is a dominated factor of the peptide-membrane binding, while the short α-helical fragments PAP(262-270) and PAP(262-272) strongly interact with the membrane at the interface, generally following to the Gibbs free energy of water-to-interface insertion. © 2013 Mendeleev Communications. All rights reserved.
dc.relation.ispartofseries	Mendeleev Communications
dc.title	Interaction of prostatic acid phosphatase fragments with a lipid bilayer as studied by NMR spectroscopy
dc.type	Article
dc.relation.ispartofseries-issue	6
dc.relation.ispartofseries-volume	23
dc.collection	Публикации сотрудников КФУ
dc.relation.startpage	313
dc.source.id	SCOPUS09599436-2013-23-6-SID84888395753

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Публикации сотрудников КФУ Scopus [24551]
Коллекция содержит публикации сотрудников Казанского федерального (до 2010 года Казанского государственного) университета, проиндексированные в БД Scopus, начиная с 1970г.