Solution of the spatial structure of dimeric transmembrane domains of proteins by heteronuclear NMR spectroscopy and molecular modeling

被引：0

作者：

Volynsky P.E. ^{[1
]}

Bocharov E.V. ^{[1
]}

Nolde D.E. ^{[1
]}

Vereschaga Ya.A. ^{[1
]}

Mayzel M.L. ^{[1
]}

Mineev K.S. ^{[1
]}

Mineeva E.A. ^{[1
]}

Pustovalova Yu.E. ^{[1
]}

Gagnidze I.A. ^{[1
]}

Efremov R.G. ^{[1
]}

Arseniev A.S. ^{[1
]}

机构：

[1] Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997

来源：

Biophysics | 2006年 / 51卷 / Suppl 1期

基金：

美国国家科学基金会;

关键词：

Glycophorin A; Membrane proteins; Membrane-mimicking media; Molecular dynamics;

D O I：

10.1134/S0006350906070050

中图分类号：

学科分类号：

摘要：

Membrane proteins play an important role in various biological processes. An approach combining NMR spectroscopy with molecular modeling was used to study the spatial structure and intramolecular dynamics of protein transmembrane domains consisting of two interacting α-helices. The approach was tested with model transmembrane domains and yielded detailed atomic-level data on the protein-protein and protein-lipid interactions. © 2006 Pleiades Publishing, Ltd.

引用

页码：23 / 27

页数：4

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