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Default The secondary structure of phospholamban: a two-dimensional NMR study.

The secondary structure of phospholamban: a two-dimensional NMR study.

Related Articles The secondary structure of phospholamban: a two-dimensional NMR study.

Biochem Biophys Res Commun. 1995 Dec 26;217(3):1200-7

Authors: Maslennikov IV, Sobol AG, Anagli J, James P, Vorherr T, Arseniev AS, Carafoli E

Phospholamban (PLN) is an intrinsic membrane protein of 52 amino acids which regulates the Ca2+ pump of the sarcoplasmic reticulum of heart, slow-twitch and smooth muscle (SR): it is normally assumed to exist in the membrane as a homopentamer. A monomeric analogue of phospholamban PLN(C41F), in which Cys41 was replaced by a Phe, was synthesized and its conformation studied by 1H NMR spectroscopy in a 1:1 mixture of chloroform/methanol. Most of the resonances in the 1H NMR spectra were assigned. The work has shown that the C-terminal hydrophobic portion forms a very stable alpha-helix. The hydrophilic N-terminal part adopts an alpha-helix configuration which is much less stable except for the stretch containing the phosphorylation sites.

PMID: 8554577 [PubMed - indexed for MEDLINE]



Source: PubMed
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