We report the solid-state 13C and 15N NMR of insoluble elastin which has been synthesized in vitro with isotopically enriched glycine. Most of the glycines reside in a domain with good cross-polarization (CP) efficiencies, although surprisingly, a portion resides in an environment that is not detectable using CP. Our data indicate that much of the 13C population resides in regions of significant conformational flexibility. To support these conclusions, we present 13C and 15N cross-polarization with magic-angle-spinning (CPMAS) data in conjunction with "direct-polarization", nonspinning CP, and T1 measurements.
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http://dx.doi.org/10.1021/ja017711x | DOI Listing |
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 PDFJ 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 PDFBiomol 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.
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