Related ArticlesNMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer beta-sheet.
J Biomol NMR. 1998 May;11(4):407-14
Authors: Pham TN, Koide S
The crystal structure of outer surface protein A (OspA) from Borrelia burgdorferi contains a single-layer beta-sheet connecting the N- and C-terminal globular domains. The central beta-sheet consists largely of polar amino acids and it is solvent-exposed on both faces, which so far appears to be unique among known protein structures. We have accomplished nearly complete backbone H, C and N and C beta/H beta assignments of OspA (28 kDa) using standard triple resonance techniques without perdeuteration. This was made possible by recording spectra at a high temperature (45 degrees C). The chemical shift index and 15N T1/T2 ratios show that both the secondary structure and the global conformation of OspA in solution are similar to the crystal structure, suggesting that the unique central beta-sheet is fairly rigid.
Real-Time NMR Studies of Electrochemical Double-Layer Capacitors
Real-Time NMR Studies of Electrochemical Double-Layer Capacitors
Hao Wang, Thomas K.-J. Ko?ster, Nicole M. Trease, Julie Se?galini, Pierre-Louis Taberna, Patrice Simon, Yury Gogotsi and Clare P. Grey
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2072115/aop/images/medium/ja-2011-072115_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2072115
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/-UeWTD49pVw
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NMR structure of an acyl-carrier protein from Borrelia burgdorferi.
NMR structure of an acyl-carrier protein from Borrelia burgdorferi.
NMR structure of an acyl-carrier protein from Borrelia burgdorferi.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt 9):1137-40
Authors: Barnwal RP, Van Voorhis WC, Varani G
Abstract
Nearly complete resonance assignment and the high-resolution NMR structure of the acyl-carrier protein from Borrelia burgdorferi, a target of the Seattle Structural Genomics Center for Infectious Disease (SSGCID) structure-determination pipeline, are reported. This protein...
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09-10-2011 06:51 PM
[NMR paper] NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins.
NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins.
Related Articles NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins.
Biophys J. 2005 Mar;88(3):2030-7
Authors: Bokor M, Csizmók V, Kovács D, Bánki P, Friedrich P, Tompa P, Tompa K
Intrinsically unstructured/disordered proteins (IUPs) exist in a disordered and largely solvent-exposed, still functional, structural state under physiological conditions. As their function is often directly linked with structural disorder,...
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[NMR paper] NMR structures of three single-residue variants of the human prion protein.
NMR structures of three single-residue variants of the human prion protein.
Related Articles NMR structures of three single-residue variants of the human prion protein.
Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8340-5
Authors: Calzolai L, Lysek DA, Guntert P, von Schroetter C, Riek R, Zahn R, Wüthrich K
The NMR structures of three single-amino acid variants of the C-terminal domain of the human prion protein, hPrP(121-230), are presented. In hPrP(M166V) and hPrP(R220K) the substitution is with the corresponding residue in murine PrP, and in...
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11-19-2010 08:29 PM
[NMR paper] Interactions of a didomain fragment of the Drosophila sex-lethal protein with single-
Interactions of a didomain fragment of the Drosophila sex-lethal protein with single-stranded uridine-rich oligoribonucleotides derived from the transformer and Sex-lethal messenger RNA precursors: NMR with residue-selective uridine substitutions.
Related Articles Interactions of a didomain fragment of the Drosophila sex-lethal protein with single-stranded uridine-rich oligoribonucleotides derived from the transformer and Sex-lethal messenger RNA precursors: NMR with residue-selective uridine substitutions.
J Biomol NMR. 2000 Jun;17(2):153-65
Authors: Kim...
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[NMR paper] NMR identification of epitopes of Lyme disease antigen OspA to monoclonal antibodies.
NMR identification of epitopes of Lyme disease antigen OspA to monoclonal antibodies.
Related Articles NMR identification of epitopes of Lyme disease antigen OspA to monoclonal antibodies.
J Mol Biol. 1998 Aug 7;281(1):61-7
Authors: Huang X, Yang X, Luft BJ, Koide S
Outer surface protein A (OspA) from the Lyme disease spirochete Borrelia burgdorferi has been a focus of vaccine development. We have identified epitopes of OspA to two monoclonal antibodies (mAbs) by comparing NMR chemical shifts of free OspA and those in Fab complexes....
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[NMR paper] NMR-based structural studies of the pNR-2/pS2 single domain trefoil peptide. Similari
NMR-based structural studies of the pNR-2/pS2 single domain trefoil peptide. Similarities to porcine spasmolytic peptide and evidence for a monomeric structure.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR-based structural studies of the pNR-2/pS2 single domain trefoil peptide. Similarities to porcine spasmolytic peptide and evidence for a monomeric structure.
Eur J Biochem. 1995 Nov 1;233(3):847-55
Authors: Polshakov VI, Frenkiel TA,...
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[NMR paper] Representing an ensemble of NMR-derived protein structures by a single structure.
Representing an ensemble of NMR-derived protein structures by a single structure.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Representing an ensemble of NMR-derived protein structures by a single structure.
Protein Sci. 1993 Jun;2(6):936-44
Authors: Sutcliffe MJ
The usefulness of representing an ensemble of...