A novel approach to solid-state NMR spectroscopy has allowed researchers to unravel structural details of bactofilin from the ulcer-causing corkscrew bacterium, Helicobacter pylori.
[NMR paper] ?-Helical architecture of cytoskeletal bactofilin filaments revealed by solid-state NMR.
?-Helical architecture of cytoskeletal bactofilin filaments revealed by solid-state NMR.
?-Helical architecture of cytoskeletal bactofilin filaments revealed by solid-state NMR.
Proc Natl Acad Sci U S A. 2014 Dec 30;
Authors: Vasa S, Lin L, Shi C, Habenstein B, Riedel D, Kühn J, Thanbichler M, Lange A
Abstract
Bactofilins are a widespread class of bacterial filament-forming proteins, which serve as cytoskeletal scaffolds in various cellular pathways. They are characterized by a conserved architecture, featuring a central...
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Unravelling proton NMR spectra of foodstuffs with independent component analysis techniques
Unravelling proton NMR spectra of foodstuffs with independent component analysis techniques
http://www.spectroscopynow.com/common/images/thumbnails/144c151d9a0.jpgOverlapping signals in the proton NMR spectra of complex liquids, like foodstuffs and soft drinks, can be processed using a chemometric method, independent component analysis, to extract the spectra of pure components and determine their concentrations.
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03-14-2014 07:34 PM
[NMR paper] NMR Study on Small Proteins from Helicobacter pylori for Antibiotic Target Discovery: A Review.
NMR Study on Small Proteins from Helicobacter pylori for Antibiotic Target Discovery: A Review.
NMR Study on Small Proteins from Helicobacter pylori for Antibiotic Target Discovery: A Review.
Molecules. 2013;18(11):13410-24
Authors: Kang SJ, Kim DH, Lee BJ
Abstract
Due to the widespread and increasing appearance of antibiotic resistance, a new strategy is needed for developing novel antibiotics. Especially, there are no specific antibiotics for Helicobacter pylori (H. pylori). H. pylori are bacteria that live in the stomach and are...
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11-02-2013 10:04 AM
[NMR paper] NMR assignments of a hypothetical pseudo-knotted protein HP0242 from Helicobacter pylori.
NMR assignments of a hypothetical pseudo-knotted protein HP0242 from Helicobacter pylori.
Related Articles NMR assignments of a hypothetical pseudo-knotted protein HP0242 from Helicobacter pylori.
Biomol NMR Assign. 2013 Jul 4;
Authors: Chien CT, Wang LW, Liu YN, Hsu BD, Lyu PC, Hsu ST
Abstract
Many knotted proteins have been discovered recently, but the folding process of which remains elusive. HP0242 is a hypothetical protein from Helicobacter pylori, which is a model system for studying the folding pathway of a knotted protein. In...
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07-05-2013 09:52 PM
[NMR paper] Overproduction of the N-terminal Anticodon-binding Domain of the Non-discriminating Aspartyl-tRNA Synthetase from Helicobacter pylori for Crystallization and NMR Measurements.
Overproduction of the N-terminal Anticodon-binding Domain of the Non-discriminating Aspartyl-tRNA Synthetase from Helicobacter pylori for Crystallization and NMR Measurements.
Overproduction of the N-terminal Anticodon-binding Domain of the Non-discriminating Aspartyl-tRNA Synthetase from Helicobacter pylori for Crystallization and NMR Measurements.
Protein Expr Purif. 2013 Feb 27;
Authors: Fuengfuloy P, Chuawong P, Suebka S, Wattana-Amorn P, Williams C, Crump MP, Songsiriritthigul C
Abstract
Aminoacyl-tRNA synthetases (aaRSs) covalently...
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03-05-2013 03:25 PM
[NMR paper] The zinc-binding fragment of HypA from Helicobacter pylori: a tempting site also for nickel ions.
The zinc-binding fragment of HypA from Helicobacter pylori: a tempting site also for nickel ions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles The zinc-binding fragment of HypA from Helicobacter pylori: a tempting site also for nickel ions.
Dalton Trans. 2013 Jan 21;
Authors: Rowinska-Zyrek M, Potocki S, Witkowska D, Valensin D, Kozlowski H
Abstract
HypA, a nickel accessory protein from H. pylori, binds a zinc ion in it's structural site, a loop with two conserved...
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02-03-2013 10:19 AM
Unravelling the Conformational Plasticity of the Extracellular Domain of a Prokaryotic nAChR Homologue in Solution by NMR
Unravelling the Conformational Plasticity of the Extracellular Domain of a Prokaryotic nAChR Homologue in Solution by NMR
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi201223u/aop/images/medium/bi-2011-01223u_0002.gif
Biochemistry
DOI: 10.1021/bi201223u
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/rGTPGWIkyp0
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10-21-2011 09:52 AM
[NMR paper] NMR assignment of the novel Helicobacter pylori protein JHP1348.
NMR assignment of the novel Helicobacter pylori protein JHP1348.
Related Articles NMR assignment of the novel Helicobacter pylori protein JHP1348.
J Biomol NMR. 2005 Jul;32(3):262
Authors: Borin BN, Popescu A, Krezel AM
Unravelling Helicobacter: Bactofilin insights from NMR
A novel approach to solid-state NMR spectroscopy has allowed researchers to unravel structural details of bactofilin from the ulcer-causing corkscrew bacterium, Helicobacter pylori.
Linear Mode
