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 [NMR paper] Anti-cancer effects of emodin on HepG2 cells as revealed by 1H-NMR based metabolic profiling. |
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Apr 21, 2018 - 10:14 AM - by nmrlearner
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Anti-cancer effects of emodin on HepG2 cells as revealed by 1H-NMR based metabolic profiling.
Related Articles Anti-cancer effects of emodin on HepG2 cells as revealed by 1H-NMR based metabolic profiling.
J Proteome Res. 2018 Apr 20;:
Authors: Xing YX, Li MH, Tao L, Ruan LY, Hong W, Chen C, Zhao WL, Xu H, Chen JF, Wang JS
Abstract
Hepatic carcinoma is one of the most common cancers in the world with a high incidence. Emodin is an anthraquinone derived from Polygonum multiflorum Thunb, possessing anti-cancer activity. The purpose of this study is to investigate the anti-cancer effect of different dosages of emodin on HepG2 cells using 1H-NMR based metabolic approach complemented with qRT-PCR and flow cytometry to identify potential markers and discover the targets to explore the underlying mechanism. Emodin can dose-dependently inhibit the growth of HepG2 cells, perturb cell cycle progression, down-regulate the expression of genes and proteins related to glycolysis and trigger intracellular ROS generation. Orthogonal signal correction partial least-squares discriminant analysis (OSC-PLS-DA) and correlation network analysis of the 1H NMR data showed significant changes in many endogenous metabolites after emodin exposure concerning oxidative stress and disturbances in amino acid and energy metabolism. These findings are helpful to understand the anti-cancer mechanism of emodin and provide a... [Read More]
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0 Replies | 1 Views
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[NMR paper] Solution NMR Studies of Anesthetic Interactions with Ion Channels. |
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Apr 21, 2018 - 10:14 AM - by nmrlearner
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Solution NMR Studies of Anesthetic Interactions with Ion Channels.
Related Articles Solution NMR Studies of Anesthetic Interactions with Ion Channels.
Methods Enzymol. 2018;603:49-66
Authors: Bondarenko V, Wells M, Xu Y, Tang P
Abstract
NMR spectroscopy is one of the major tools to provide atomic resolution protein structural information. It has been used to elucidate the molecular details of interactions between anesthetics and ion channels, to identify anesthetic binding sites, and to characterize channel dynamics and changes introduced by anesthetics. In this chapter, we present solution NMR methods essential for investigating interactions between ion channels and general anesthetics, including both volatile and intravenous anesthetics. Case studies are provided with a focus on pentameric ligand-gated ion channels and the voltage-gated sodium channel NaChBac.
PMID: 29673534 [PubMed - in process]
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0 Replies | 1 Views
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Primary Transfer Step in the Light-Driven Ion Pump Bacteriorhodopsin: An Irreversible U-Turn Revealed by Dynamic Nuclear Polarization-Enhanced Magic Angle Spinning NMR #DNPNMR |
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Apr 20, 2018 - 2:17 PM - by nmrlearner
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From The DNP-NMR Blog:
Primary Transfer Step in the Light-Driven Ion Pump Bacteriorhodopsin: An Irreversible U-Turn Revealed by Dynamic Nuclear Polarization-Enhanced Magic Angle Spinning NMR #DNPNMR
Ni, Q.Z., et al., Primary Transfer Step in the Light-Driven Ion Pump Bacteriorhodopsin: An Irreversible U-Turn Revealed by Dynamic Nuclear Polarization-Enhanced Magic Angle Spinning NMR. J. Am. Chem. Soc., 2018. 140(11): p. 4085-4091.
https://www.ncbi.nlm.nih.gov/pubmed/29489362
Despite much attention, the path of the highly consequential primary proton transfer in the light-driven ion pump bacteriorhodopsin (bR) remains mysterious. Here we use DNP-enhanced magic angle spinning (MAS) NMR to study critical elements of the active site just before the Schiff base (SB) deprotonates (in the L intermediate), immediately after the SB has deprotonated and Asp85 has become protonated (in the Mo intermediate), and just after the SB has reprotonated and Asp96 has deprotonated (in the N intermediate). An essential feature that made these experiments possible is the 75-fold signal enhancement through DNP. (15)N(SB)-(1)H correlations reveal that the newly deprotonated SB is accepting a hydrogen bond from an alcohol and (13)C-(13)C correlations show that Asp85 draws close to Thr89 before the primary proton transfer. Concurrently, (15)N-(13)C correlations between the SB and Asp85 show that helices C and G draw closer together just prior to the proton transfer and relax thereafter. Together, these results indicate that Thr89... [Read More]
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0 Replies | 9 Views
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[NMR paper] Parallel ?-Sheet Structure of Alanine Tetrapeptide in the Solid State As Studied by Solid-State NMR Spectroscopy. |
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Apr 19, 2018 - 1:52 PM - by nmrlearner
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Parallel ?-Sheet Structure of Alanine Tetrapeptide in the Solid State As Studied by Solid-State NMR Spectroscopy.
 Related Articles Parallel ?-Sheet Structure of Alanine Tetrapeptide in the Solid State As Studied by Solid-State NMR Spectroscopy.
J Phys Chem B. 2016 09 01;120(34):8932-41
Authors: Asakura T, Horiguchi K, Aoki A, Tasei Y, Naito A
Abstract
The structural analysis of alanine oligopeptides is important for understanding the crystalline region in silks from spiders and wild silkworms and also the mechanism of cellular toxicity of human diseases arising from expansion in polyalanine sequences. The atomic-level structures of alanine tripeptide and tetrapeptide with antiparallel ?-sheet structures (AP-Ala3 and AP-Ala4, respectively) together with alanine tripeptide with parallel ?-sheet structures (P-Ala3) have been determined, but alanine tetrapeptide with a parallel ?-sheet structure (P-Ala4) has not been reported yet. In this article, first, we established the preparation protocol of P-Ala4 from more stable AP-Ala4. Second, complete assignments of the (13)C,... [Read More]
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