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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http://dx.doi.org/10.1007/s12104-010-9285-y | DOI Listing |
Biomol NMR Assign
December 2024
Institute of Medical Biochemistry, Federal University of Rio de Janeiro, Rio de Janeiro, RJ, Brazil.
J-domain proteins (JDPs) are essential cochaperones of heat shock protein 70 (Hsp70), as they bind and deliver misfolded polypeptides while also stimulating ATPase activity, thereby mediating the refolding process and assisting Hsp70 in maintaining cellular proteostasis. Despite their importance, detailed structural information about JDP‒Hsp70 complexes is still being explored due to various technical challenges. One major challenge is the lack of more detailed structural data on full-length JDPs.
View Article and Find Full Text PDFWater Res
December 2024
School of Water Resources and Environment and Research Center of Environmental Science and Engineering, Sino-Hungarian Joint Laboratory of Environmental Science and Health, China University of Geosciences (Beijing), 29 Xueyuan Road, Haidian District, 100083 Beijing, China; Department of Technical Biogeochemistry, Helmholtz Centre for Environmental Research-UFZ, Permoserstraße 15 04318 Leipzig, Germany; Isodetect GmbH, Deutscher Platz 5b, 04103 Leipzig, Germany. Electronic address:
This study investigates carbon, hydrogen, nitrogen and chlorine isotope fractionation during the transformation of 3-chloroaniline (3-CA) via direct photolysis, TiO photocatalytic degradation at neutral condition and hydrolysis at pH 3, pH 7 and pH 11. Direct photolysis and ∙OH reaction (UV/HO) showed similar inverse isotope fractionation (ε) for carbon (1.9 ± 0.
View Article and Find Full Text PDFBiomol NMR Assign
December 2024
NMR Laboratory, Medical Physics Department, Institute of Physics, Kazan Federal University, Kremlevskaya Str., 18, Kazan, 420008, Russia.
Biomol NMR Assign
December 2024
Institute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe University, Max-von-Laue-Str. 7, 60438, Frankfurt/Main, Germany.
Ephrin receptors regulate intercellular communication and are thus involved in tumor development. Ephrin receptor A2 (EphA2), in particular, is overexpressed in a variety of cancers and is a proven target for anti-cancer drugs. The N-terminal ligand-binding domain of ephrin receptors is responsible for the recognition of their ligands, ephrins, and is directly involved in receptor activation.
View Article and Find Full Text PDFInt J Mol Sci
November 2024
Department of Biochemistry, University of Toronto, Toronto, ON M5S 1A1, Canada.
L-arginine: glycine amidinotransferase (AGAT) gained academic interest as the rate-limiting enzyme in creatine biosynthesis and its role in the regulation of creatine homeostasis. Of clinical relevance is the diagnosis of patients with AGAT deficiency but also the potential role of AGAT as therapeutic target for the treatment of another creatine deficiency syndrome, guanidinoacetate N-methyltransferase (GAMT) deficiency. Applying a stable isotope-labeled substrate method, we utilized ARG 15N (ARG-δ2) and GLY 13C15N (GLY-δ3) to determine the rate of 1,2-13C,15N guanidinoacetate (GAA-δ5) formation to assess AGAT activity in various mouse tissue samples and human-derived cells.
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