Dimeric structure of the transmembrane domain of glycophorin a in lipidic and detergent environments.

ABSTRACT: Specific interactions between transmembrane α-helices, to a large extent, determine the biological function of integral membrane proteins upon normal development and in pathological states of an organism. Various membrane-like media, partially those mimicking the conditions of multicomponent biological membranes, are used to study the structural and thermodynamic features that define the character of oligomerization of transmembrane helical segments. The choice of the composition of the membrane-mimicking medium is conducted in an effort to obtain a biologically relevant conformation of the protein complex and a sample that would be stable enough to allow to perform a series of long-term experiments with its use. In the present work, heteronuclear NMR spectroscopy and molecular dynamics si

SUBMITTER: Mineev KS 

PROVIDER: S-EPMC3347579 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature