NMR Solution Structure and Extracellular Loop Dynamics of the Outer Membrane Protein OprG of Pseudomonas Aeruginosa Explain Transport of Small Amino Acids
NMR Solution Structure and Extracellular Loop Dynamics of the Outer Membrane Protein OprG of Pseudomonas Aeruginosa Explain Transport of Small Amino Acids
Publication date: 16 February 2016 Source:Biophysical Journal, Volume 110, Issue 3, Supplement 1
Author(s): Iga Kucharska, Patrick Seelheim, Thomas Edrington, Binyong Liang, Lukas K. Tamm
[NMR paper] NMR solution structure of the terminal immunoglobulin-like domain from the Leptospira host-interacting outer membrane protein, LigB.
NMR solution structure of the terminal immunoglobulin-like domain from the Leptospira host-interacting outer membrane protein, LigB.
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Biochemistry. 2014 Jul 28;
Authors: Ptak CP, Hsieh CL, Lin YP, Maltsev AS, Raman R, Sharma Y, Oswald RE, Chang YF
Abstract
A number of surface proteins specific to pathogenic strains of Leptospira have been identified. The Lig protein family has shown...
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[NMR paper] Structure optimization of 2-benzamidobenzoic acids as PqsD inhibitors for Pseudomonas aeruginosa infections and elucidation of binding mode by SPR, STD NMR, and molecular docking.
Structure optimization of 2-benzamidobenzoic acids as PqsD inhibitors for Pseudomonas aeruginosa infections and elucidation of binding mode by SPR, STD NMR, and molecular docking.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Structure optimization of 2-benzamidobenzoic acids as PqsD inhibitors for Pseudomonas aeruginosa infections and elucidation of binding mode by SPR, STD NMR, and molecular docking.
J Med Chem. 2013 Aug 8;56(15):6146-55
Authors: Weidel E, de Jong JC, Brengel...
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[NMR paper] High-resolution NMR reveals secondary structure and folding of amino Acid transporter from outer chloroplast membrane.
High-resolution NMR reveals secondary structure and folding of amino Acid transporter from outer chloroplast membrane.
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PLoS One. 2013;8(10):e78116
Authors: Zook JD, Molugu TR, Jacobsen NE, Lin G, Soll J, Cherry BR, Brown MF, Fromme P
Abstract
Solving high-resolution structures for membrane proteins continues to be a daunting challenge in the structural biology community. In this study we report our...
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Molecular dynamics re-refinement of two different small RNA loop structures using the original NMR data suggest a common structure
Molecular dynamics re-refinement of two different small RNA loop structures using the original NMR data suggest a common structure
Abstract Restrained molecular dynamics simulations are a robust, though perhaps underused, tool for the end-stage refinement of biomolecular structures. We demonstrate their utilityâ??using modern simulation protocols, optimized force fields, and inclusion of explicit solvent and mobile counterionsâ??by re-investigating the solution structures of two RNA hairpins that had previously been refined using conventional techniques. The structures, both domain 5...
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06-25-2012 04:41 AM
[NMR paper] Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza
Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR.
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FEBS Lett. 2003 Nov 27;555(1):139-43
Authors: Tamm LK, Abildgaard F, Arora A, Blad H, Bushweller JH
Recent progress from our laboratories to determine structures of small membrane proteins (up to 20 kDa) in detergent micelles...
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11-24-2010 09:16 PM
[NMR paper] The solution conformations of amino acids from molecular dynamics simulations of Gly-
The solution conformations of amino acids from molecular dynamics simulations of Gly-X-Gly peptides: comparison with NMR parameters.
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Biochem Cell Biol. 1998;76(2-3):164-70
Authors: van der Spoel D
The conformations that amino acids can adopt in the random coil state are of fundamental interest in the context of protein folding research and studies of protein-peptide interactions. To date, no...
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11-17-2010 11:06 PM
[NMR paper] Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determine
Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determined by two-dimensional 1H NMR.
Related Articles Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determined by two-dimensional 1H NMR.
Biochemistry. 1991 Sep 17;30(37):9040-6
Authors: Detlefsen DJ, Thanabal V, Pecoraro VL, Wagner G
The solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa based on 2D 1H NMR data is reported. Two sets of structure calculations were completed with a combination of simulated annealing...
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08-21-2010 11:12 PM
[NMR paper] Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determine
Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determined by two-dimensional 1H NMR.
Related Articles Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determined by two-dimensional 1H NMR.
Biochemistry. 1991 Sep 17;30(37):9040-6
Authors: Detlefsen DJ, Thanabal V, Pecoraro VL, Wagner G
The solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa based on 2D 1H NMR data is reported. Two sets of structure calculations were completed with a combination of simulated annealing...
NMR Solution Structure and Extracellular Loop Dynamics of the Outer Membrane Protein OprG of Pseudomonas Aeruginosa Explain Transport of Small Amino Acids
Linear Mode
