NMR studies and molecular dynamics simulation of cyclosporin in complex with detergent micelles

dc.contributor.author	Efimov S.
dc.contributor.author	Klochkov V.
dc.date.accessioned	2018-09-18T20:35:34Z
dc.date.available	2018-09-18T20:35:34Z
dc.date.issued	2012
dc.identifier.uri	https://dspace.kpfu.ru/xmlui/handle/net/141472
dc.description.abstract	Cyclosporin A is a highly hydrophobic peptide, but its complex with sodium dodecyl sulphate micelles can be readily dissolved in water. Nuclear magnetic resonance (NMR) investigations of cyclosporin bound to detergent micelles were carried out (including NOE spectroscopy) and yielded internuclear distances for a set of atom pairs. Based on these structural data, conformation of cyclosporin was obtained by means of molecular dynamics simulation.
dc.subject	Model membrane
dc.subject	Molecular dynamics simulation
dc.subject	NOE spectroscopy
dc.subject	Peptide conformation
dc.title	NMR studies and molecular dynamics simulation of cyclosporin in complex with detergent micelles
dc.type	Article
dc.relation.ispartofseries-issue	2
dc.relation.ispartofseries-volume	14
dc.collection	Публикации сотрудников КФУ
dc.relation.startpage	12202
dc.source.id	SCOPUS-2012-14-2-SID84871627177

Files in this item

Name: SCOPUS-2012-14-2- ...

Size: 43.02Kb

Format: PDF

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