title: The secondary structure of phospholamban: a two-dimensional NMR study.
abstract: 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.
authors.affiliation: Shemyakin & Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
authors.forename: I V
authors.initials: IV
authors.lastname: Maslennikov
authors.forename: A G
authors.initials: AG
authors.lastname: Sobol
authors.forename: J
authors.initials: J
authors.lastname: Anagli
authors.forename: P
authors.initials: P
authors.lastname: James
authors.forename: T
authors.initials: T
authors.lastname: Vorherr
authors.forename: A S
authors.initials: AS
authors.lastname: Arseniev
authors.forename: E
authors.initials: E
authors.lastname: Carafoli
mesh_terms: D000595:Amino Acid Sequence; D002135:Calcium-Binding Proteins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008565:Membrane Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D009124:Muscle Proteins / Q000737:chemistry; D010750:Phosphoproteins / Q000737:chemistry; D017433:Protein Structure, Secondary; D000099211:Phospholamban
chemical_list: D002135:Calcium-Binding Proteins; D008565:Membrane Proteins; D009124:Muscle Proteins; D010750:Phosphoproteins; D000099211:Phospholamban