Phospholamban structural dynamics in lipid bilayers probed by a spin label rigidly coupled to the peptide backbone
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Mobility of TOAC spin-labelled peptides binding to the Src SH3 domain studied by paramagnetic NMRTOAC spin labels in the backbone of alamethicin: EPR studies in lipid membranesStructure and topology of monomeric phospholamban in lipid membranes determined by a hybrid solution and solid-state NMR approachStructures of the Excited States of Phospholamban and Shifts in Their Populations upon PhosphorylationStructural Dynamics and Topology of Phosphorylated Phospholamban Homopentamer Reveal Its Role in the Regulation of Calcium TransportProbing topology and dynamics of the second transmembrane domain (M2δ) of the acetyl choline receptor using magnetically aligned lipid bilayers (bicelles) and EPR spectroscopy.Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy.The alpha-helical propensity of the cytoplasmic domain of phospholamban: a molecular dynamics simulation of the effect of phosphorylation and mutation.An allosteric mechanism inferred from molecular dynamics simulations on phospholamban pentamer in lipid membranesEffects of CMAP and electrostatic cutoffs on the dynamics of an integral membrane protein: the phospholamban study.Effect of membrane thickness on conformational sampling of phospholamban from computer simulations.Mapping the interaction surface of a membrane protein: unveiling the conformational switch of phospholamban in calcium pump regulation.Internal dynamics of a supramolecular nanofibre.(1)H/(15)N heteronuclear NMR spectroscopy shows four dynamic domains for phospholamban reconstituted in dodecylphosphocholine micelles.Dipolar coupling between nitroxide spin labels: the development and application of a tether-in-a-cone model.Synthetic phosphopeptides enable quantitation of the content and function of the four phosphorylation states of phospholamban in cardiac muscleInteractions between Ca2+-ATPase and the pentameric form of phospholamban in two-dimensional co-crystalsEffects of naturally occurring arginine 14 deletion on phospholamban conformational dynamics and membrane interactionsDynamics and conformational studies of TOAC spin labeled analogues of Ctx(Ile(21))-Ha peptide from Hypsiboas albopunctatus.A spirocyclohexyl nitroxide amino acid spin label for pulsed EPR spectroscopy distance measurements.Pulse dipolar ESR of doubly labeled mini TAR DNA and its annealing to mini TAR RNAAtomic-level mechanisms for phospholamban regulation of the calcium pump.Spectroscopic validation of the pentameric structure of phospholambanRotational dynamics of phospholamban determined by multifrequency electron paramagnetic resonance.Protein-protein interactions in calcium transport regulation probed by saturation transfer electron paramagnetic resonance.The structural topology of wild-type phospholamban in oriented lipid bilayers using 15N solid-state NMR spectroscopyTuning the structural coupling between the transmembrane and cytoplasmic domains of phospholamban to control sarcoplasmic reticulum Ca(2+)-ATPase (SERCA) function.A bifunctional spin label reports the structural topology of phospholamban in magnetically-aligned bicelles.Cardiac myosin binding protein-C restricts intrafilament torsional dynamics of actin in a phosphorylation-dependent manner.Determining the topology of integral membrane peptides using EPR spectroscopy.Structural and dynamic basis of phospholamban and sarcolipin inhibition of Ca(2+)-ATPase.Cell death versus cell survival instructed by supramolecular cohesion of nanostructuresProtein structural dynamics revealed by site-directed spin labeling and multifrequency EPR.The spin label amino acid TOAC and its uses in studies of peptides: chemical, physicochemical, spectroscopic, and conformational aspects.Structural dynamics of muscle protein phosphorylation.Functions of intrinsic disorder in transmembrane proteins.(15)N Solid-state NMR spectroscopic studies on phospholamban at its phosphorylated form at ser-16 in aligned phospholipid bilayers.Lipid-mediated folding/unfolding of phospholamban as a regulatory mechanism for the sarcoplasmic reticulum Ca2+-ATPasePhosphomimetic mutations increase phospholamban oligomerization and alter the structure of its regulatory complex.Phospholamban oligomerization, quaternary structure, and sarco(endo)plasmic reticulum calcium ATPase binding measured by fluorescence resonance energy transfer in living cells.
P2860
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P2860
Phospholamban structural dynamics in lipid bilayers probed by a spin label rigidly coupled to the peptide backbone
description
article científic
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article scientifique
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articolo scientifico
@it
artigo científico
@pt
bilimsel makale
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scientific article published on 24 September 2004
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Phospholamban structural dynam ...... oupled to the peptide backbone
@en
Phospholamban structural dynam ...... upled to the peptide backbone.
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type
label
Phospholamban structural dynam ...... oupled to the peptide backbone
@en
Phospholamban structural dynam ...... upled to the peptide backbone.
@nl
prefLabel
Phospholamban structural dynam ...... oupled to the peptide backbone
@en
Phospholamban structural dynam ...... upled to the peptide backbone.
@nl
P2093
P2860
P356
P1476
Phospholamban structural dynam ...... oupled to the peptide backbone
@en
P2093
Christine B Karim
David D Thomas
Tara L Kirby
Yuri Nesmelov
Zhiwen Zhang
P2860
P304
14437-14442
P356
10.1073/PNAS.0402801101
P407
P577
2004-09-24T00:00:00Z