[NMR paper] Assessing Interactions Between a Polytopic Membrane Protein and Lipid Bilayers Using Differential Scanning Calorimetry and Solid-State NMR.
Related ArticlesAssessing Interactions Between a Polytopic Membrane Protein and Lipid Bilayers Using Differential Scanning Calorimetry and Solid-State NMR.
J Phys Chem B. 2018 Feb 19;:
Authors: Banigan JR, Leninger M, Her AS, Traaseth NJ
Abstract
It is known that the lipid composition within a cellular membrane can influence membrane protein structure and function. In this Article, we investigated how structural changes to a membrane protein upon substrate binding can impact the lipid bilayer. To carry out this study, we reconstituted the secondary active drug transporter EmrE into a variety of phospholipid bilayers varying in headgroup and chain length and carried out differential scanning calorimetry (DSC) and solid-state NMR experiments. The DSC results revealed a difference in cooperativity of the lipid phase transition for drug-free EmrE protonated at glutamic acid 14 (i.e., proton-loaded form) and the tetraphenylphosphonium (TPP+) bound form of the protein (i.e., drug-loaded form). To complement these findings, we acquired magic-angle-spinning (MAS) spectra in the presence and absence of TPP+ by directly probing the phospholipid headgroup using 31P NMR. These spectra showed a reduction in lipid line widths around the main phase transition for samples where EmrE was bound to TPP+ compared to the drug free form. Finally, we collected oriented solid-state NMR spectra on isotopically enriched EmrE that displayed chemical shift perturbations to both transmembrane and loop residues upon TPP+ binding. All of these results prompt us to propose a mechanism whereby substrate-induced changes to the structural dynamics of EmrE alters the surrounding lipids within the bilayer.
PMID: 29457729 [PubMed - as supplied by publisher]
[NMR paper] Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR.
Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR.
Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR.
Proc Natl Acad Sci U S A. 2017 Nov 20;:
Authors: Elkins MR, Williams JK, Gelenter MD, Dai P, Kwon B, Sergeyev IV, Pentelute BL, Hong M
Abstract
The influenza M2 protein not only forms a proton channel but also mediates membrane scission in a cholesterol-dependent manner to cause virus budding and release. The atomic interaction of cholesterol...
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11-22-2017 02:01 PM
[NMR paper] Correlating Lipid Bilayer Fluidity with Sensitivity and Resolution of Polytopic Membrane Protein Spectra by Solid-State NMR Spectroscopy.
Correlating Lipid Bilayer Fluidity with Sensitivity and Resolution of Polytopic Membrane Protein Spectra by Solid-State NMR Spectroscopy.
Related Articles Correlating Lipid Bilayer Fluidity with Sensitivity and Resolution of Polytopic Membrane Protein Spectra by Solid-State NMR Spectroscopy.
Biochim Biophys Acta. 2014 May 13;
Authors: Banigan JR, Gayen A, Traaseth NJ
Abstract
Solid-state NMR spectroscopy has emerged as an excellent tool to study the structure and dynamics of membrane proteins under native-like conditions in lipid...
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05-20-2014 11:10 PM
Correlating Lipid Bilayer Fluidity with Sensitivity and Resolution of Polytopic Membrane Protein Spectra by Solid-State NMR Spectroscopy
Correlating Lipid Bilayer Fluidity with Sensitivity and Resolution of Polytopic Membrane Protein Spectra by Solid-State NMR Spectroscopy
Publication date: Available online 13 May 2014
Source:Biochimica et Biophysica Acta (BBA) - Biomembranes</br>
Author(s): James R. Banigan , Anindita Gayen , Nathaniel J. Traaseth</br>
Solid-state NMR spectroscopy has emerged as an excellent tool to study the structure and dynamics of membrane proteins under native-like conditions in lipid bilayers. One of the key considerations in experimental design is the uniaxial rotational...
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05-14-2014 04:50 AM
[NMR paper] Paramagnetic doping of a 7TM membrane protein in lipid bilayers by Gd(3+)-complexes for solid-state NMR spectroscopy.
Paramagnetic doping of a 7TM membrane protein in lipid bilayers by Gd(3+)-complexes for solid-state NMR spectroscopy.
Related Articles Paramagnetic doping of a 7TM membrane protein in lipid bilayers by Gd(3+)-complexes for solid-state NMR spectroscopy.
J Biomol NMR. 2013 Dec 4;
Authors: Ullrich SJ, Hölper S, Glaubitz C
Abstract
A considerable limitation of NMR spectroscopy is its inherent low sensitivity. Approximately 90*% of the measuring time is used by the spin system to return to its Boltzmann equilibrium after excitation, which is...
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[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
Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers
Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers
Abstract Oriented solid-state NMR is the most direct methodology to obtain the orientation of membrane proteins with respect to the lipid bilayer. The method consists of measuring 1H-15N dipolar couplings (DC) and 15N anisotropic chemical shifts (CSA) for membrane proteins that are uniformly aligned with respect to the membrane bilayer. A significant advantage of this approach is that tilt and azimuthal...
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[NMR paper] 13C NMR, X-ray, and differential scanning calorimetry investigations of truncated BPT
13C NMR, X-ray, and differential scanning calorimetry investigations of truncated BPTI (aprotinin) analogues.
Related Articles 13C NMR, X-ray, and differential scanning calorimetry investigations of truncated BPTI (aprotinin) analogues.
Biochemistry. 1998 Mar 17;37(11):3645-53
Authors: Hansen PE, Zhang W, Lauritzen C, Bjørn S, Petersen LC, Norris K, Olsen OH, Betzel C
Truncated BPTI missing residues 1 and 2 is investigated together with variants thereof (Lys-15, Arg-17, and Arg-42 are replaced by other residues in various combinations). A...
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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...
Assessing Interactions Between a Polytopic Membrane Protein and Lipid Bilayers Using Differential Scanning Calorimetry and Solid-State NMR.
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