Related ArticlesThe 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.
[NMR paper] NMR solution structure and topological orientation of monomeric phospholamban in dode
NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles.
Related Articles NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles.
Biophys J. 2003 Oct;85(4):2589-98
Authors: Zamoon J, Mascioni A, Thomas DD, Veglia G
Phospholamban is an integral membrane protein that regulates the contractility of cardiac muscle by maintaining cardiomyocyte calcium homeostasis. Abnormalities in association of protein kinase A with PLB have recently...
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[NMR paper] Two-dimensional NMR study of the heme active site structure of chloroperoxidase.
Two-dimensional NMR study of the heme active site structure of chloroperoxidase.
Related Articles Two-dimensional NMR study of the heme active site structure of chloroperoxidase.
J Biol Chem. 2003 Mar 7;278(10):7765-74
Authors: Wang X, Tachikawa H, Yi X, Manoj KM, Hager LP
The heme active site structure of chloroperoxidase (CPO), a glycoprotein that displays versatile catalytic activities isolated from the marine mold Caldariomyces fumago, has been characterized by two-dimensional NMR spectroscopic studies. All hyperfine shifted resonances...
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[NMR paper] Secondary structure of myristoylated recoverin determined by three-dimensional hetero
Secondary structure of myristoylated recoverin determined by three-dimensional heteronuclear NMR: implications for the calcium-myristoyl switch.
Related Articles Secondary structure of myristoylated recoverin determined by three-dimensional heteronuclear NMR: implications for the calcium-myristoyl switch.
Biochemistry. 1994 Sep 6;33(35):10743-53
Authors: Ames JB, Tanaka T, Stryer L, Ikura M
Recoverin, a new member of the EF-hand superfamily, serves as a Ca2+ sensor in vision. A myristoyl or related N-acyl group is covalently attached at its...
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[NMR paper] NMR determination of the secondary structure and the three-dimensional polypeptide ba
NMR determination of the secondary structure and the three-dimensional polypeptide backbone fold of the human sterol carrier protein 2.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR determination of the secondary structure and the three-dimensional polypeptide backbone fold of the human sterol carrier protein 2.
FEBS Lett. 1993 Nov 29;335(1):18-26
Authors: Szyperski T, Scheek S, Johansson J, Assmann G, Seedorf U, Wüthrich K
Nuclear magnetic resonance (NMR)...
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[NMR paper] Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using
Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide.
Related Articles Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide.
Biochemistry. 1992 Sep 22;31(37):8790-8
Authors: Sönnichsen FD, Van Eyk JE, Hodges RS, Sykes BD
The structure of a synthetic peptide comprising the 28 amino-terminal residues of actin has been examined by 1H-NMR and CD spectroscopy. The peptide is largely unstructured and flexible in solution but becomes...
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[NMR paper] Secondary structure of a complement control protein module by two-dimensional 1H NMR.
Secondary structure of a complement control protein module by two-dimensional 1H NMR.
Related Articles Secondary structure of a complement control protein module by two-dimensional 1H NMR.
Biochemistry. 1991 Jan 29;30(4):997-1004
Authors: Barlow PN, Baron M, Norman DG, Day AJ, Willis AC, Sim RB, Campbell ID
The complement control protein (CCP) module (also known as the short consensus repeat) is a consensus sequence of about 60 amino acid residues which is thought to fold independently. It occurs over 140 times in more than 20 extracellular...
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[NMR paper] A two-dimensional 1H-NMR study on Megasphaera elsdenii flavodoxin in the oxidized sta
A two-dimensional 1H-NMR study on Megasphaera elsdenii flavodoxin in the oxidized state and some comparisons with the two-electron-reduced state.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles A two-dimensional 1H-NMR study on Megasphaera elsdenii flavodoxin in the oxidized state and some comparisons with the two-electron-reduced state.
Eur J Biochem. 1990 Nov 26;194(1):199-216
Authors: van Mierlo CP, van der Sanden BP, van Woensel P,...
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[NMR paper] Two-dimensional NMR studies and secondary structure of cobrotoxin in aqueous solution
Two-dimensional NMR studies and secondary structure of cobrotoxin in aqueous solution.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Two-dimensional NMR studies and secondary structure of cobrotoxin in aqueous solution.
Eur J Biochem. 1990 Nov 13;193(3):789-99
Authors: Yu C, Lee CS, Chuang LC, Shei YR, Wang CY
The 1H-NMR spectra of cobrotoxin, a neurotoxic protein isolated from Formosan cobra Naja naja atra, have been studied by...
The secondary structure of phospholamban: a two-dimensional NMR study.
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