Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1023/B:JNMR.0000012844.21707.8c | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
NMR 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.
View Article and Find Full Text PDFBackbone NMR resonance assignment of Sis1, a type B J-domain protein from Saccharomyces cerevisiae.
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 PDFCorrection: H, C, and N resonance assignments of the amyloidogenic peptide SEM2(49-107) by NMR spectroscopy.
Biomol NMR Assign
December 2024
NMR Laboratory, Medical Physics Department, Institute of Physics, Kazan Federal University, Kremlevskaya Str., 18, Kazan, 420008, Russia.
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!