ArticleJournal of the American Chemical Society2011
Paramagnetic-based NMR restraints lift residual dipolar coupling degeneracy in multidomain detergent-solubilized membrane proteins.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed.
- Utilizing Molecular Dynamics Simulations, Machine Learning, Cryo-EM, and NMR Spectroscopy to Predict and Validate Protein Dynamics.International journal of molecular sciences · 2024Review
- Reconstruction of Coupled Intra- and Interdomain Protein Motion from Nuclear and Electron Magnetic Resonance.Journal of the American Chemical Society · 2021Article
- Partial alignment, residual dipolar couplings and molecular symmetry in solution NMR.Journal of biomolecular NMR · 2019Article
- Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Chemical reviews · 2018Review
- Utilization of paramagnetic relaxation enhancements for structural analysis of actin-binding proteins in complex with actin.Scientific reports · 2016Article
- The PRE-Derived NMR Model of the 38.8-kDa Tri-Domain IsdH Protein from Staphylococcus aureus Suggests That It Adaptively Recognizes Human Hemoglobin.Journal of molecular biology · 2016Article
- A mechanism for the auto-inhibition of hyperpolarization-activated cyclic nucleotide-gated (HCN) channel opening and its relief by cAMP.The Journal of biological chemistry · 2014Article
- Allosteric regulation of SERCA by phosphorylation-mediated conformational shift of phospholamban.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Determination of structural topology of a membrane protein in lipid bilayers using polarization optimized experiments (POE) for static and MAS solid state NMR spectroscopy.Journal of biomolecular NMR · 2013Article
- Structures of the excited states of phospholamban and shifts in their populations upon phosphorylation.Biochemistry · 2013Article
- Solution NMR studies on the orientation of membrane-bound peptides and proteins by paramagnetic probes.Molecules (Basel, Switzerland) · 2013Review
- Investigation of the Polymeric Properties of α-Synuclein and Comparison with NMR Experiments: A Replica Exchange Molecular Dynamics Study.Journal of chemical theory and computation · 2012Article
- Identification and removal of nitroxide spin label contaminant: impact on PRE studies of α-helical membrane proteins in detergent.Protein science : a publication of the Protein Society · 2012Article
- Isotope labeling for solution and solid-state NMR spectroscopy of membrane proteins.Advances in experimental medicine and biology · 2012Review
- Topology and immersion depth of an integral membrane protein by paramagnetic rates from dissolved oxygen.Journal of biomolecular NMR · 2011Article
- Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
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6 authors.
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Abstract
Residual dipolar couplings (RDCs) are widely used as orientation-dependent NMR restraints to improve the resolution of the NMR conformational ensemble of biomacromolecules and define the relative orientation of multidomain proteins and protein complexes. However, the interpretation of RDCs is complicated by the intrinsic degeneracy of analytical solutions and protein dynamics that lead to ill-defined orientations of the structural domains (ghost orientations). Here, we illustrate how restraints from paramagnetic relaxation enhancement (PRE) experiments lift the orientational ambiguity of multidomain membrane proteins solubilized in detergent micelles. We tested this approach on monomeric phospholamban (PLN), a 52-residue membrane protein, which is composed of two helical domains connected by a flexible loop. We show that the combination of classical solution NMR restraints (NOEs and dihedral angles) with RDC and PRE constraints resolves topological ambiguities, improving the convergence of the PLN structural ensemble and giving the depth of insertion of the protein within the micelle. The combination of RDCs with PREs will be necessary for improving the accuracy and precision of membrane protein conformational ensembles, where three-dimensional structures are dictated by interactions with the membrane-mimicking environment rather than compact tertiary folds common in globular proteins.
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