[NMR paper] Secondary Structure, Backbone Dynamics and Structural Topology of Phospholamban and Its Phosphorylated and Arg9Cys Mutated Forms in Phospholipid Bilayers Utilizing (13)C and (15)N Solid-state NMR Spectroscopy.
Secondary Structure, Backbone Dynamics and Structural Topology of Phospholamban and Its Phosphorylated and Arg9Cys Mutated Forms in Phospholipid Bilayers Utilizing (13)C and (15)N Solid-state NMR Spectroscopy.
Secondary Structure, Backbone Dynamics and Structural Topology of Phospholamban and Its Phosphorylated and Arg9Cys Mutated Forms in Phospholipid Bilayers Utilizing (13)C and (15)N Solid-state NMR Spectroscopy.
J Phys Chem B. 2014 Feb 10;
Authors: Yu X, Lorigan GA
Abstract
Phospholamban (PLB) is a membrane protein that regulates heart muscle relaxation rates via interactions with the sarcoplasmic reticulum Ca2+ ATPase (SERCA). When PLB is phosphorylated or Arg9Cys (R9C) mutated, inhibition of SERCA is relieved. 13C and 15N solid-state NMR spectroscopy is utilized to investigate conformational changes of PLB upon phosphorylation and R9C mutation. 13C=O NMR spectra of the cytoplasmic domain reveal two ?-helical structural components with population changes upon phosphorylation and R9C mutation. The appearance of an unstructured component is observed on domain Ib. 15N NMR spectra indicate an increase in backbone dynamics of the cytoplasmic domain. Wild-type PLB (WT-PLB), Ser16 phosphorylated PLB (P-PLB) and R9C mutated PLB (R9C-PLB) all have a very dynamic domain Ib and the transmembrane domain has an immobile component. 15N NMR spectra indicate that the cytoplasmic domain of R9C-PLB adopts an orientation similar to P-PLB and shifts away from the membrane surface. Domain Ib (Leu28) of P-PLB and R9C-PLB loses the alignment. The R9C-PLB adopts a conformation similar to P-PLB with a population shift to a more extended and disordered state. The NMR data suggests the more extended and disorder forms of PLB may relate to inhibition relief.
PMID: 24511878 [PubMed - as supplied by publisher]
[NMR paper] Determination of structural topology of a membrane protein in lipid bilayers using polarization optimized experiments (POE) for static and MAS solid state NMR spectroscopy.
Determination of structural topology of a membrane protein in lipid bilayers using polarization optimized experiments (POE) for static and MAS solid state NMR spectroscopy.
Determination of structural topology of a membrane protein in lipid bilayers using polarization optimized experiments (POE) for static and MAS solid state NMR spectroscopy.
J Biomol NMR. 2013 Aug 21;
Authors: Mote KR, Gopinath T, Veglia G
Abstract
The low sensitivity inherent to both the static and magic angle spinning techniques of solid-state NMR (ssNMR) spectroscopy...
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08-23-2013 01:07 AM
[NMR paper] Probing the Interaction of Arg9Cys Mutated Phospholamban with Phospholipid Bilayers by Solid-state NMR Spectroscopy.
Probing the Interaction of Arg9Cys Mutated Phospholamban with Phospholipid Bilayers by Solid-state NMR Spectroscopy.
Related Articles Probing the Interaction of Arg9Cys Mutated Phospholamban with Phospholipid Bilayers by Solid-state NMR Spectroscopy.
Biochim Biophys Acta. 2013 Jul 9;
Authors: Yu X, Lorigan GA
Abstract
Phospholamban (PLB) is a 52 amino acid integral membrane protein that interacts with the sarcoplasmic reticulum Ca(2+) ATPase (SERCA) and helps to regulate Ca(2+) flow. PLB inhibits SERCA impairing Ca(2+) translocation. The...
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07-16-2013 09:04 PM
[NMR paper] Aggregation and dynamics of oligocholate transporters in phospholipid bilayers revealed by solid-state NMR spectroscopy.
Aggregation and dynamics of oligocholate transporters in phospholipid bilayers revealed by solid-state NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Aggregation and dynamics of oligocholate transporters in phospholipid bilayers revealed by solid-state NMR spectroscopy.
Langmuir. 2012 Dec 11;28(49):17071-8
Authors: Wang T, Widanapathirana L, Zhao Y, Hong M
Abstract
Macrocycles made of cholate building blocks were previously found to...
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05-22-2013 04:43 PM
Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method [Biophysics and Computational Biology]
Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method
Verardi, R., Shi, L., Traaseth, N. J., Walsh, N., Veglia, G....
Date: 2011-05-31
Phospholamban (PLN) is a type II membrane protein that inhibits the sarcoplasmic reticulum Ca2+-ATPase (SERCA), thereby regulating calcium homeostasis in cardiac muscle. In membranes, PLN forms pentamers that have been proposed to function either as a storage for active monomers or as ion channels. Here, we report the T-state structure of pentameric PLN solved by a hybrid solution and...
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05-31-2011 11:41 PM
Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method.
Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method.
Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method.
Proc Natl Acad Sci U S A. 2011 May 16;
Authors: Verardi R, Shi L, Traaseth NJ, Walsh N, Veglia G
Phospholamban (PLN) is a type II membrane protein that inhibits the sarcoplasmic reticulum Ca(2+)-ATPase (SERCA), thereby regulating calcium homeostasis in cardiac muscle. In membranes, PLN forms pentamers that have been proposed...
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05-19-2011 04:20 AM
[NMR paper] Solid-state NMR measurements of the kinetics of the interaction between phospholamban and Ca2+-ATPase in lipid bilayers.
Solid-state NMR measurements of the kinetics of the interaction between phospholamban and Ca2+-ATPase in lipid bilayers.
Related Articles Solid-state NMR measurements of the kinetics of the interaction between phospholamban and Ca2+-ATPase in lipid bilayers.
Mol Membr Biol. 2005 Jul-Aug;22(4):353-61
Authors: Hughes E, Middleton DA
Phospholamban (PLB) is a small transmembrane protein that regulates calcium transport across the sarcoplasmic reticulum (SR) of cardiac cells via a reversible inhibitory interaction with Ca2+-ATPase. In this work...
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12-01-2010 06:56 PM
[NMR paper] Probing the oligomeric state of phospholamban variants in phospholipid bilayers from
Probing the oligomeric state of phospholamban variants in phospholipid bilayers from solid-state NMR measurements of rotational diffusion rates.
Related Articles Probing the oligomeric state of phospholamban variants in phospholipid bilayers from solid-state NMR measurements of rotational diffusion rates.
Biochemistry. 2005 Mar 15;44(10):4055-66
Authors: Hughes E, Clayton JC, Middleton DA
Phospholamban (PLB) is a small transmembrane protein that regulates calcium transport across the sarcoplasmic reticulum (SR) of cardiac cells. PLB...
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11-24-2010 11:14 PM
Lipid-Protein Correlations in Nanoscale Phospholipid Bilayers by Solid-State NMR.
Lipid-Protein Correlations in Nanoscale Phospholipid Bilayers by Solid-State NMR.
Lipid-Protein Correlations in Nanoscale Phospholipid Bilayers by Solid-State NMR.
Biochemistry. 2010 Aug 30;
Authors: Kijac A, Shih AY, Nieuwkoop AJ, Schulten K, Sligar SG, Rienstra CM
Nanodiscs are an example of discoidal nanoscale lipid/protein particles that have been extremely useful for the biochemical and biophysical characterization of membrane proteins. They are discoidal lipid bilayer fragments encircled and stabilized by two amphipathic helical...
Secondary Structure, Backbone Dynamics and Structural Topology of Phospholamban and Its Phosphorylated and Arg9Cys Mutated Forms in Phospholipid Bilayers Utilizing (13)C and (15)N Solid-state NMR Spectroscopy.
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