ArticleBiochimica et biophysica acta2012
Probing the helical tilt and dynamic properties of membrane-bound phospholamban in magnetically aligned bicelles using electron paramagnetic resonance spectroscopy.
Article in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Pathological mutations in the phospholamban cytoplasmic region affect its topology and dynamics modulating the extent of SERCA inhibition.Biochimica et biophysica acta. Biomembranes · 2024Article
- Solid-State NMR Study to Probe the Effects of Divalent Metal Ions (CaLangmuir : the ACS journal of surfaces and colloids · 2021Article
- Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Chemical reviews · 2018Review
- TMPL: a database of experimental and theoretical transmembrane protein models positioned in the lipid bilayer.Database : the journal of biological databases and curation · 2017Article
- A bifunctional spin label reports the structural topology of phospholamban in magnetically-aligned bicelles.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2016Article
- Optimization of bicelle lipid composition and temperature for EPR spectroscopy of aligned membranes.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Correlating lipid bilayer fluidity with sensitivity and resolution of polytopic membrane protein spectra by solid-state NMR spectroscopy.Biochimica et biophysica acta · 2015Article
- Effects of naturally occurring arginine 14 deletion on phospholamban conformational dynamics and membrane interactions.Biochimica et biophysica acta · 2015Article
- Secondary structure, backbone dynamics, and structural topology of phospholamban and its phosphorylated and Arg9Cys-mutated forms in phospholipid bilayers utilizing 13C and 15N solid-state NMR spectroscopy.The journal of physical chemistry. B · 2014Article
- Probing the interaction of Arg9Cys mutated phospholamban with phospholipid bilayers by solid-state NMR spectroscopy.Biochimica et biophysica acta · 2013Article
- When detergent meets bilayer: birth and coming of age of lipid bicelles.Progress in nuclear magnetic resonance spectroscopy · 2013Review
- The magic of bicelles lights up membrane protein structure.Chemical reviews · 2012Review
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Authors and funding
7 authors.
Funding
Abstract
Wild-type phospholamban (WT-PLB), a Ca(2+)-ATPase (SERCA) regulator in the sarcoplasmic reticulum membrane, was studied using TOAC nitroxide spin labeling, magnetically aligned bicelles, and electron paramagnetic resonance (EPR) spectroscopy to ascertain structural and dynamic information. Different structural domains of PLB (transmembrane segment: positions 42 and 45, loop region: position 20, and cytoplasmic domain: position 10) were probed with rigid TOAC spin labels to extract the transmembrane helical tilt and structural dynamic information, which is crucial for understanding the regulatory function of PLB in modulating Ca(2+)-ATPase activity. Aligned experiments indicate that the transmembrane domain of wild-type PLB has a helical tilt of 13°±4° in DMPC/DHPC bicelles. TOAC spin labels placed on the WT-PLB transmembrane domain showed highly restricted motion with more than 100ns rotational correlation time (τ(c)); whereas the loop, and the cytoplasmic regions each consists of two distinct motional dynamics: one fast component in the sub-nanosecond scale and the other component is slower dynamics in the nanosecond range.
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