[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.
Related Articles NMR solution structure of the terminal immunoglobulin-like domain from the Leptospira host-interacting outer membrane protein, LigB.
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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The Core of Ure2p Prion Fibrils Is Formed by the N-Terminal Segment in a Parallel Cross-? Structure: Evidence from Solid-State NMR.
The Core of Ure2p Prion Fibrils Is Formed by the N-Terminal Segment in a Parallel Cross-? Structure: Evidence from Solid-State NMR.
The Core of Ure2p Prion Fibrils Is Formed by the N-Terminal Segment in a Parallel Cross-? Structure: Evidence from Solid-State NMR.
J Mol Biol. 2011 Apr 8;
Authors: Kryndushkin DS, Wickner RB, Tycko R
Intracellular fibril formation by Ure2p produces the non-Mendelian genetic element in Saccharomyces cerevisiae, making Ure2p a prion protein. We show that solid-state NMR spectra of full-length Ure2p fibrils, seeded...
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04-19-2011 11:01 PM
[NMR paper] NMR structures of the C-terminal segment of surfactant protein B in detergent micelle
NMR structures of the C-terminal segment of surfactant protein B in detergent micelles and hexafluoro-2-propanol.
Related Articles NMR structures of the C-terminal segment of surfactant protein B in detergent micelles and hexafluoro-2-propanol.
Biochemistry. 2004 Dec 7;43(48):15187-94
Authors: Booth V, Waring AJ, Walther FJ, Keough KM
Although the membrane-associated surfactant protein B (SP-B) is an essential component of lung surfactant, which is itself essential for life, the molecular basis for its activity is not understood. SP-B's...
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11-24-2010 10:03 PM
[NMR paper] NMR evidence for progressive stabilization of native-like structure upon aggregation
NMR evidence for progressive stabilization of native-like structure upon aggregation of acid-denatured LysN.
Related Articles NMR evidence for progressive stabilization of native-like structure upon aggregation of acid-denatured LysN.
J Mol Biol. 2000 Jan 14;295(2):239-55
Authors: Alexandrescu AT, Lamour FP, Jaravine VA
The acid-denatured form of the protein LysN aggregates reversibly at pH 2.0. The strength of self-association increases with increasing Cl(-) anion concentration. At low concentrations of protein or Cl(-) anion, resonances of...
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[NMR paper] NMR study suggests a major role for Arg111 in maintaining the structure and dynamical
NMR study suggests a major role for Arg111 in maintaining the structure and dynamical properties of type II human cellular retinoic acid binding protein.
Related Articles NMR study suggests a major role for Arg111 in maintaining the structure and dynamical properties of type II human cellular retinoic acid binding protein.
Biochemistry. 1998 Sep 15;37(37):13021-32
Authors: Wang L, Yan H
The solution structure of a site-directed mutant of type-II human cellular retinoic acid binding protein (CRABPII) with Arg111 replaced by methionine (R111M)...
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11-17-2010 11:15 PM
[NMR paper] Photoreceptor rhodopsin: structural and conformational study of its chromophore 11-ci
Photoreceptor rhodopsin: structural and conformational study of its chromophore 11-cis retinal in oriented membranes by deuterium solid state NMR.
Related Articles Photoreceptor rhodopsin: structural and conformational study of its chromophore 11-cis retinal in oriented membranes by deuterium solid state NMR.
FEBS Lett. 1998 Jan 30;422(2):201-4
Authors: Gröbner G, Choi G, Burnett IJ, Glaubitz C, Verdegem PJ, Lugtenburg J, Watts A
Rhodopsin is the retinal photoreceptor responsible for visual signal transduction. To determine the orientation and...
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11-17-2010 11:06 PM
[NMR paper] Light-induced membrane protein phosphorylation in the bovine rod outer segment. A mag
Light-induced membrane protein phosphorylation in the bovine rod outer segment. A magic angle spinning 31P-NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Light-induced membrane protein phosphorylation in the bovine rod outer segment. A magic angle spinning 31P-NMR study.
Biophys Chem. 1990 May;36(1):27-31
Authors: Albert AD, Frye JS, Yeagle PL
Magic angle spinning 31P-NMR (MAS 31P-NMR) spectra of bovine rod outer segments, unphosphorylated and...
Progressive Rod–Cone Degeneration (PRCD) ProteinRequires N-Terminal S-Acylation and Rhodopsin Bindingfor Photoreceptor Outer Segment Localization and Maintaining IntracellularStability
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