Mapping the interaction sites between membrane spanning proteins is a key challenge in structural biology. In this study a carbene footprinting approach is developed and applied to identify the interfacial sites of a trimeric, integral membrane protein, OmpF, solubilised in micelles. The diazirine-based footprinting probe is effectively sequestered by, and incorporated into, the micelles leading to efficient labelling of the membrane-spanning regions of the protein upon irradiation at 349 nm. Areas associated with protein-protein interactions between the trimer subunits remained unlabelled, thus revealing their location.
[NMR paper] Solid-state NMR provides evidence for small-amplitude slow domain motions in a multi-spanning transmembrane ?-helical protein.
Solid-state NMR provides evidence for small-amplitude slow domain motions in a multi-spanning transmembrane ?-helical protein.
Solid-state NMR provides evidence for small-amplitude slow domain motions in a multi-spanning transmembrane ?-helical protein.
J Am Chem Soc. 2017 Jun 14;
Authors: Good D, Pham C, Jagas J, Lewandowski JR, Ladizhansky V
Abstract
Proteins are dynamic entities and populate ensembles of conformations. Transitions between states within a conformational ensemble occur over a broad spectrum of amplitude...
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06-15-2017 03:37 PM
[NMR paper] NMR Insight into Myosin-Binding Subunit Coiled Coil Structure Reveals Binding Interface with Protein Kinase G-I? Leucine Zipper in Vascular Function.
NMR Insight into Myosin-Binding Subunit Coiled Coil Structure Reveals Binding Interface with Protein Kinase G-I? Leucine Zipper in Vascular Function.
Related Articles NMR Insight into Myosin-Binding Subunit Coiled Coil Structure Reveals Binding Interface with Protein Kinase G-I? Leucine Zipper in Vascular Function.
J Biol Chem. 2017 Mar 09;:
Authors: Sharma AK, Birrane GG, Anklin C, Rigby AC, Alper SL
Abstract
Nitrovasodilators relax vascular smooth muscle cells (VSMC) in part by modulating the interaction of the C-terminal...
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03-11-2017 05:12 PM
Dynamic nuclear polarization of membrane proteins: covalently bound spin-labels at protein-protein interfaces
From The DNP-NMR Blog:
Dynamic nuclear polarization of membrane proteins: covalently bound spin-labels at protein-protein interfaces
Wylie, B.J., et al., Dynamic nuclear polarization of membrane proteins: covalently bound spin-labels at protein-protein interfaces. J Biomol NMR, 2015. 61(3-4): p. 361-7.
http://www.ncbi.nlm.nih.gov/pubmed/25828256
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06-17-2015 09:27 PM
Dynamic nuclear polarization of membrane proteins: covalently bound spin-labels at proteinā??protein interfaces
Dynamic nuclear polarization of membrane proteins: covalently bound spin-labels at proteinā??protein interfaces
Abstract
We demonstrate that dynamic nuclear polarization of membrane proteins in lipid bilayers may be achieved using a novel polarizing agent: pairs of spin labels covalently bound to a protein of interest interacting at an intermolecular interaction surface. For gramicidin A, nitroxide tags attached to the N-terminal intermolecular interface region become proximal only when bimolecular channels forms in the membrane. We obtained signal...
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04-01-2015 08:27 AM
Hydration dynamics as an intrinsic ruler for refining protein structure at lipid membrane interfaces
From The DNP-NMR Blog:
Hydration dynamics as an intrinsic ruler for refining protein structure at lipid membrane interfaces
Cheng, C.-Y., et al., Hydration dynamics as an intrinsic ruler for refining protein structure at lipid membrane interfaces. Proc. Nat. Aca. Sci. USA, 2013. 110(42): p. 16838-16843.
http://www.pnas.org/content/110/42/16838.abstract
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07-31-2014 01:45 AM
[NMR paper] An NMR method for the determination of protein-binding interfaces using dioxygen-indu
An NMR method for the determination of protein-binding interfaces using dioxygen-induced spin-lattice relaxation enhancement.
Related Articles An NMR method for the determination of protein-binding interfaces using dioxygen-induced spin-lattice relaxation enhancement.
J Am Chem Soc. 2005 Apr 27;127(16):5826-32
Authors: Sakakura M, Noba S, Luchette PA, Shimada I, Prosser RS
Using oxygen as a paramagnetic probe, researchers can routinely study topologies and protein-binding interfaces by NMR. The paramagnetic contribution to the amide (1)H...
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11-25-2010 08:21 PM
[NMR paper] Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the
Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the three amino-terminal zinc finger domains from transcription factor IIIA.
Related Articles Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the three amino-terminal zinc finger domains from transcription factor IIIA.
J Biomol NMR. 1998 Jul;12(1):51-71
Authors: Foster MP, Wuttke DS, Clemens KR, Jahnke W, Radhakrishnan I, Tennant L, Reymond M, Chung J, Wright PE
We report the NMR resonance assignments for a macromolecular...
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11-17-2010 11:15 PM
[NMR paper] Prion protein fragments spanning helix 1 and both strands of beta sheet (residues 125
Prion protein fragments spanning helix 1 and both strands of beta sheet (residues 125-170) show evidence for predominantly helical propensity by CD and NMR.
Related Articles Prion protein fragments spanning helix 1 and both strands of beta sheet (residues 125-170) show evidence for predominantly helical propensity by CD and NMR.
Fold Des. 1998;3(5):313-20
Authors: Sharman GJ, Kenward N, Williams HE, Landon M, Mayer RJ, Searle MS
BACKGROUND: Transmissible spongiform encephalopathies are a group of neurodegenerative disorders of man and animals...
Carbene footprinting reveals binding interfaces of a multimeric membrane spanning protein
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