(1)H, (13)C and (15)N assignment of the GNA1946 outer membrane lipoprotein from Neisseria meningitidis

GNA1946 (Genome-derived Neisseria Antigen 1946) is a highly conserved exposed outer membrane lipoprotein from Neisseria meningitidis bacteria of 287 amino acid length (31 kDa). Although the structure of NMB1946 has been solved recently by X-Ray crystallography, understanding the behaviour of GNA1946...

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Autores principales: Neumoin, A., Leonchiks, A., Petit, P., Vuillard, L., Pizza, M., Soriani, M., Boelens, R., Bonvin, A. M. J. J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2010
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3166609/
https://www.ncbi.nlm.nih.gov/pubmed/21188561
http://dx.doi.org/10.1007/s12104-010-9285-y
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author Neumoin, A.
Leonchiks, A.
Petit, P.
Vuillard, L.
Pizza, M.
Soriani, M.
Boelens, R.
Bonvin, A. M. J. J.
author_facet Neumoin, A.
Leonchiks, A.
Petit, P.
Vuillard, L.
Pizza, M.
Soriani, M.
Boelens, R.
Bonvin, A. M. J. J.
author_sort Neumoin, A.
collection PubMed
description GNA1946 (Genome-derived Neisseria Antigen 1946) is a highly conserved exposed outer membrane lipoprotein from Neisseria meningitidis bacteria of 287 amino acid length (31 kDa). Although the structure of NMB1946 has been solved recently by X-Ray crystallography, understanding the behaviour of GNA1946 in aqueuos solution is highly relevant for the discovery of the antigenic determinants of the protein that will possibly lead to a more efficient vaccine development against virulent serogroup B strain of N.meningitidis. Here we report almost complete (1)H, (13)C and (15)N resonance assignments of GNA1946 (residues 10–287) in aqueous buffer solution.
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spelling pubmed-31666092011-09-26 (1)H, (13)C and (15)N assignment of the GNA1946 outer membrane lipoprotein from Neisseria meningitidis Neumoin, A. Leonchiks, A. Petit, P. Vuillard, L. Pizza, M. Soriani, M. Boelens, R. Bonvin, A. M. J. J. Biomol NMR Assign Article GNA1946 (Genome-derived Neisseria Antigen 1946) is a highly conserved exposed outer membrane lipoprotein from Neisseria meningitidis bacteria of 287 amino acid length (31 kDa). Although the structure of NMB1946 has been solved recently by X-Ray crystallography, understanding the behaviour of GNA1946 in aqueuos solution is highly relevant for the discovery of the antigenic determinants of the protein that will possibly lead to a more efficient vaccine development against virulent serogroup B strain of N.meningitidis. Here we report almost complete (1)H, (13)C and (15)N resonance assignments of GNA1946 (residues 10–287) in aqueous buffer solution. Springer Netherlands 2010-12-28 2011 /pmc/articles/PMC3166609/ /pubmed/21188561 http://dx.doi.org/10.1007/s12104-010-9285-y Text en © The Author(s) 2010 https://creativecommons.org/licenses/by-nc/4.0/ This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited.
spellingShingle Article
Neumoin, A.
Leonchiks, A.
Petit, P.
Vuillard, L.
Pizza, M.
Soriani, M.
Boelens, R.
Bonvin, A. M. J. J.
(1)H, (13)C and (15)N assignment of the GNA1946 outer membrane lipoprotein from Neisseria meningitidis
title (1)H, (13)C and (15)N assignment of the GNA1946 outer membrane lipoprotein from Neisseria meningitidis
title_full (1)H, (13)C and (15)N assignment of the GNA1946 outer membrane lipoprotein from Neisseria meningitidis
title_fullStr (1)H, (13)C and (15)N assignment of the GNA1946 outer membrane lipoprotein from Neisseria meningitidis
title_full_unstemmed (1)H, (13)C and (15)N assignment of the GNA1946 outer membrane lipoprotein from Neisseria meningitidis
title_short (1)H, (13)C and (15)N assignment of the GNA1946 outer membrane lipoprotein from Neisseria meningitidis
title_sort (1)h, (13)c and (15)n assignment of the gna1946 outer membrane lipoprotein from neisseria meningitidis
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3166609/
https://www.ncbi.nlm.nih.gov/pubmed/21188561
http://dx.doi.org/10.1007/s12104-010-9285-y
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