Related ArticlesNMR assignment of the amylase-binding protein A from Streptococcus parasanguinis.
Biomol NMR Assign. 2014 Jul 14;
Authors: Liu B, Zhu F, Wu H, Matthews S
Abstract
Streptococcus parasanguinis is a primary colonizer of tooth surfaces in the oral cavity. Amylase-binding protein A (AbpA) from S. parasanguinis is responsible for the recruitment of salivary amylase to bacterial surface, which plays an important role in the development of oral biofilms. Here, we describe the essentially complete NMR assignments for AbpA.
PMID: 25016927 [PubMed - as supplied by publisher]
[NMR paper] Solution NMR assignment of LpoB, an outer-membrane anchored Penicillin-Binding Protein activator from Escherichia coli.
Solution NMR assignment of LpoB, an outer-membrane anchored Penicillin-Binding Protein activator from Escherichia coli.
Related Articles Solution NMR assignment of LpoB, an outer-membrane anchored Penicillin-Binding Protein activator from Escherichia coli.
Biomol NMR Assign. 2014 Apr 2;
Authors: Jean NL, Bougault CM, Egan AJ, Vollmer W, Simorre JP
Abstract
Bacteria surround their cytoplasmic membrane with the essential heteropolymer peptidoglycan (PG), which is made of glycan chains cross-linked by short peptides, to...
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[NMR paper] Solution structure of the Big domain from Streptococcus pneumoniae reveals a novel Ca(2+)-binding module.
Solution structure of the Big domain from Streptococcus pneumoniae reveals a novel Ca(2+)-binding module.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_npg.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Solution structure of the Big domain from Streptococcus pneumoniae reveals a novel Ca(2+)-binding module.
Sci Rep. 2013;3:1079
Authors: Wang T, Zhang J, Zhang X, Xu C, Tu X
Abstract
Streptococcus pneumoniae is a...
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[NMR paper] NMR assignment of the R2 domain of pneumococcal choline binding protein A (CbpA).
NMR assignment of the R2 domain of pneumococcal choline binding protein A (CbpA).
Related Articles NMR assignment of the R2 domain of pneumococcal choline binding protein A (CbpA).
J Biomol NMR. 2005 May;32(1):93
Authors: Luo R, Mann B, Tuomanen E, Kriwacki RW
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[NMR paper] NMR assignment and structural characterization of the fatty acid binding protein from
NMR assignment and structural characterization of the fatty acid binding protein from the flight muscle of Locusta migratoria.
Related Articles NMR assignment and structural characterization of the fatty acid binding protein from the flight muscle of Locusta migratoria.
J Biomol NMR. 2003 Apr;25(4):355-6
Authors: Lücke C, Kizilbash N, van Moerkerk HT, Veerkamp JH, Hamilton JA
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[NMR paper] NMR assignment of the A form of the pheromone-binding protein of Bombyx mori.
NMR assignment of the A form of the pheromone-binding protein of Bombyx mori.
Related Articles NMR assignment of the A form of the pheromone-binding protein of Bombyx mori.
J Biomol NMR. 2001 Jan;19(1):79-80
Authors: Horst R, Damberger F, Peng G, Nikonova L, Leal WS, Wüthrich K
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[NMR paper] Structure and dynamic properties of the single disulfide-deficient alpha-amylase inhi
Structure and dynamic properties of the single disulfide-deficient alpha-amylase inhibitor tendamistat: an NMR study.
Related Articles Structure and dynamic properties of the single disulfide-deficient alpha-amylase inhibitor tendamistat: an NMR study.
Proteins. 1998 Nov 1;33(2):285-94
Authors: Balbach J, Seip S, Kessler H, Scharf M, Kashani-Poor N, Engels JW
Covalent linkages such as disulfide bonds are important for the stabilization of proteins. In the present NMR study we compare the structure and the dynamics of the single...
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11-17-2010 11:15 PM
[NMR paper] 1H NMR studies of the mercuric ion binding protein MerP: sequential assignment, secon
1H NMR studies of the mercuric ion binding protein MerP: sequential assignment, secondary structure and global fold of oxidized MerP.
Related Articles 1H NMR studies of the mercuric ion binding protein MerP: sequential assignment, secondary structure and global fold of oxidized MerP.
J Biomol NMR. 1993 Nov;3(6):613-26
Authors: Eriksson PO, Sahlman L
The oxidized form of the mercuric ion binding protein MerP has been studied by two-dimensional NMR. MerP, which is a periplasmic water-soluble protein with 72 amino acids, is involved in the...
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Structural analysis of the exopolysaccharide produced by Streptococcus thermophilus S
Abstract The use of lactic acid bacteria in fermentation of milk results in favorable physical and rheological properties due to in situ exopolysaccharide (EPS) production. The EPS from S. thermophilus ST1 produces highly viscous aqueous solutions and its structure has been investigated by NMR spectroscopy. Notably, all aspects of the elucidation of its primary structure including component analysis and absolute configuration of the constituent monosaccharides were carried out by NMR spectroscopy. An array of techniques was utilized including, inter alia, PANSY and NOESY-HSQC TILT...