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H, N, C backbone resonance assignment of human Alkbh7.
Biomol NMR Assign
January 2025
Department of Chemistry, Iowa State University, Hach Hall, 2438 Pammel Drive, Ames, IA, 50011, USA.
The Alkbh7 protein, a member of the Alkylation B (AlkB) family of dioxygenases, plays a crucial role in epigenetic regulation of cellular metabolism. This paper focuses on the NMR backbone resonance assignment of Alkbh7, a fundamental step in understanding its three-dimensional structure and dynamic behavior at the atomic level. Herein, we report the backbone H, N, C chemical shift assignment of the full-length human Alkbh7.
View Article and Find Full Text PDFBackbone and Sidechain H, N and C Resonance Assignments of a Multidrug Efflux Membrane Protein using Solution and Solid-State NMR.
bioRxiv
January 2025
Department of Biochemistry, University of Wisconsin-Madison, Madison, WI, 53706 USA.
EmrE is a bacterial membrane-embedded multidrug transporter that functions as an asymmetric homodimer. EmrE is implicated in antibiotic resistance, but is now known to confer either resistance or susceptibility depending on the identity of the small molecule substrate. Here, we report both solution- and solid-state NMR assignments of S64V-EmrE at pH 5.
View Article and Find Full Text PDFNMR spectroscopic studies of chitin oligomers - Resolution of individual residues and characterization of minor amide cis conformations.
Carbohydr Polym
March 2025
Department of Molecular Sciences, Swedish University of Agricultural Sciences, Almas Allé 5, Uppsala 75651, Sweden. Electronic address:
Chitin is the second most abundant biopolymer in nature after cellulose and is composed of N-acetylglucosamine (GlcNAc) connected via β(1 → 4)-glycosidic bonds. Despite its prominence in nature and diverse roles in pharmaceutical and food technological applications, there is still a need to develop methods to study structure and function of chitin and its corresponding oligomers. Efforts have been made to analyse chitin oligomers by NMR spectroscopy, but spectral overlap has prevented any differentiation between the interior residues.
View Article and Find Full Text PDFAssignment of the N-terminal domain of mouse cGAS.
Biomol NMR Assign
January 2025
Department of Chemistry and Chemical Biology, TU Dortmund University, Dortmund, Germany.
Cyclic GMP-AMP synthase (cGAS) is a DNA-sensing enzyme that is a member of the nucleotidyltransferase (NTase) family and functions as a DNA sensor. The protein is comprised of a catalytic NTase core domain and an unstructured hypervariable N-terminal domain (NTD) that was reported to increase protein activity by providing an additional DNA-binding surface. We report nearly complete H, N, and C backbone chemical-shift assignments of mouse cGAS NTD (residues 5-146), obtained with a set of 3D and 4D solution NMR experiments.
View Article and Find Full Text PDFRelaxation-optimized correlation spectroscopy ROCSY for assigning H or C spin systems in large proteins.
J Magn Reson
December 2024
Department of Medicine, University of Alberta, Canada; Department of Biochemistry, University of Alberta, Canada. Electronic address:
Solution NMR studies of large systems are hampered by rapid signal decay. We hereby introduce ROCSY (relaxation-optimized total correlation spectroscopy), which maximizes transfer efficiency across J-coupling-connected spin networks by minimizing the amount of time magnetization spends in the transverse plane. Hard pulses are substituted into the Clean-CITY TOCSY pulse element first developed by Ernst and co-workers, allowing for longer delays in which magnetization is aligned along the z-axis.
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