[NMR paper] The NMR structure of the sensory domain of the membranous two-component fumarate sens
The NMR structure of the sensory domain of the membranous two-component fumarate sensor (histidine protein kinase) DcuS of Escherichia coli.
The NMR structure of the sensory domain of the membranous two-component fumarate sensor (histidine protein kinase) DcuS of Escherichia coli.
J Biol Chem. 2003 Oct 3;278(40):39185-8
Authors: Pappalardo L, Janausch IG, Vijayan V, Zientz E, Junker J, Peti W, Zweckstetter M, Unden G, Griesinger C
The structure of the water-soluble, periplasmic domain of the fumarate sensor DcuS (DcuS-pd) has been determined...
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11-24-2010 09:16 PM
Membrane Alignment of the Pore-Forming Component TatA(d) of the Twin-Arginine Translo
Membrane Alignment of the Pore-Forming Component TatA(d) of the Twin-Arginine Translocase from Bacillus subtilis Resolved by Solid-State NMR Spectroscopy.
Related Articles Membrane Alignment of the Pore-Forming Component TatA(d) of the Twin-Arginine Translocase from Bacillus subtilis Resolved by Solid-State NMR Spectroscopy.
J Am Chem Soc. 2010 Oct 26;
Authors: Walther TH, Grage SL, Roth N, Ulrich AS
The twin-arginine translocase (Tat) provides protein export in bacteria and plant chloroplasts and is capable of transporting fully folded...
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Membrane Alignment of the Pore-Forming Component TatAd of the Twin-Arginine Transloca
Membrane Alignment of the Pore-Forming Component TatAd of the Twin-Arginine Translocase from Bacillus subtilis Resolved by Solid-State NMR Spectroscopy
Torsten H. Walther, Stephan L. Grage, Nadine Roth and Anne S. Ulrich
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja106963s/aop/images/medium/ja-2010-06963s_0001.gif
Journal of the American Chemical Society
DOI: 10.1021/ja106963s
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10-27-2010 08:51 AM
Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport S
Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport System from Gram-Positive Bacterium Bacillus subtilis.
Related Articles Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport System from Gram-Positive Bacterium Bacillus subtilis.
J Am Chem Soc. 2010 Aug 20;
Authors: Hu Y, Zhao E, Li H, Xia B, Jin C
The twin-arginine transport (Tat) system translocates folded proteins across the bacterial cytoplasmic or chloroplast thylakoid membrane of plants. The Tat system in most Gram-positive...
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08-25-2010 02:04 PM
[NMR paper] Solution structure of phenol hydroxylase protein component P2 determined by NMR spect
Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy.
Biochemistry. 1997 Jan 21;36(3):495-504
Authors: Qian H, Edlund U, Powlowski J, Shingler V, Sethson I
Phenol hydroxylase from Pseudomonas sp. CF600 is a member of a family of binuclear iron-center-containing multicomponent oxygenases, which catalyzes the...
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08-22-2010 03:31 PM
[NMR paper] Solution structure of phenol hydroxylase protein component P2 determined by NMR spect
Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy.
Biochemistry. 1997 Jan 21;36(3):495-504
Authors: Qian H, Edlund U, Powlowski J, Shingler V, Sethson I
Phenol hydroxylase from Pseudomonas sp. CF600 is a member of a family of binuclear iron-center-containing multicomponent oxygenases, which catalyzes the...
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08-22-2010 03:03 PM
[NMR paper] Na(+)-H+ and Na(+)-Li+ exchange are mediated by the same membrane transport protein i
Na(+)-H+ and Na(+)-Li+ exchange are mediated by the same membrane transport protein in human red blood cells: an NMR investigation.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Na(+)-H+ and Na(+)-Li+ exchange are mediated by the same membrane transport protein in human red blood cells: an NMR investigation.
Biochemistry. 1996 Sep 24;35(38):12433-42
Authors: Chi Y, Mo S, Mota de Freitas D
Na(+)-H+ exchange is a transport system present in erythrocytes which plays an important role in...
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08-22-2010 02:20 PM
[NMR paper] Solution structure of component B from methane monooxygenase derived through heteronu
Solution structure of component B from methane monooxygenase derived through heteronuclear NMR and molecular modeling.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of component B from methane monooxygenase derived through heteronuclear NMR and molecular modeling.
Biochemistry. 1999 May 4;38(18):5799-812
Authors: Chang SL, Wallar BJ, Lipscomb JD, Mayo KH
Methane monooxygenase (MMO) is a nonheme iron-containing enzyme which consists of three protein components: a...
Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport S
Journal of the American Chemical Society, Volume 0, Issue 0, Articles ASAP (As Soon As Publishable). 
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