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[NMR paper] Anti-cancer effects of emodin on HepG2 cells as revealed by 1H-NMR based metabolic profiling.
Apr 21, 2018 - 10:14 AM - by nmrlearner
nmrlearner's Avatar 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]
0 Replies | 7 Views
[NMR paper] Solution NMR Studies of Anesthetic Interactions with Ion Channels.
Apr 21, 2018 - 10:14 AM - by nmrlearner
nmrlearner's Avatar 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 | 4 Views
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
Apr 20, 2018 - 2:17 PM - by nmrlearner
nmrlearner's Avatar 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]
0 Replies | 16 Views
Pressure control helps NMR analyze protein as it folds - Chemical & Engineering News
Apr 20, 2018 - 1:59 AM - by nmrlearner
nmrlearner's Avatar Pressure control helps NMR analyze protein as it folds - Chemical & Engineering News


Chemical & Engineering News


Pressure control helps NMR analyze protein as it folds
Chemical & Engineering News
The methodology makes it possible to determine atomic-resolution structures of folding intermediates and to study disease-related events such as protein aggregation and fibril formation. ??The importance of the work is clear when one considers the ...


... [Read More]
0 Replies | 21 Views
[NMR paper] Parallel ?-Sheet Structure of Alanine Tetrapeptide in the Solid State As Studied by Solid-State NMR Spectroscopy.
Apr 19, 2018 - 1:52 PM - by nmrlearner
nmrlearner's Avatar 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]
0 Replies | 19 Views
[NMR paper] Effect of Saturated Very Long-Chain Fatty Acids on the Organization of Lipid Membranes: A Study Combining (2)H NMR Spectroscopy and Molecular Dynamics Simulations.
Apr 19, 2018 - 1:52 PM - by nmrlearner
nmrlearner's Avatar Effect of Saturated Very Long-Chain Fatty Acids on the Organization of Lipid Membranes: A Study Combining (2)H NMR Spectroscopy and Molecular Dynamics Simulations.

Related Articles Effect of Saturated Very Long-Chain Fatty Acids on the Organization of Lipid Membranes: A Study Combining (2)H NMR Spectroscopy and Molecular Dynamics Simulations.

J Phys Chem B. 2016 07 21;120(28):6951-60

Authors: Paz Ramos A, Lage P, Lamoureux G, Lafleur M

Abstract
Little is known about the interaction of very long-chain saturated fatty acids (VLCFAs) with biological membranes. However, this could play an important role on interleaflet interactions and signal transduction mechanisms in cells. The aim of this work is to determine how VLCFA structurally adapts in fluid phospholipid bilayers, since both species must exhibit a significant hydrophobic mismatch. The membrane organization has been described by means of (2)H NMR and molecular dynamics simulations. Our results show that the protonation state affects the position and order of free fatty acids (FFAs) in phospholipid membranes. It... [Read More]
0 Replies | 17 Views
[NMR paper] Structure and Dynamic Properties of a Ti-Binding Peptide Bound to TiO2 Nanoparticles As Accessed by (1)H NMR Spectroscopy.
Apr 19, 2018 - 1:52 PM - by nmrlearner
nmrlearner's Avatar Structure and Dynamic Properties of a Ti-Binding Peptide Bound to TiO2 Nanoparticles As Accessed by (1)H NMR Spectroscopy.

Related Articles Structure and Dynamic Properties of a Ti-Binding Peptide Bound to TiO2 Nanoparticles As Accessed by (1)H NMR Spectroscopy.

J Phys Chem B. 2016 05 26;120(20):4600-7

Authors: Suzuki Y, Shindo H, Asakura T

Abstract
Saturation transfer difference (STD) NMR spectroscopy is a powerful method for detecting and characterizing ligand-receptor interactions. In this study, the STD method was used to characterize the interactions of a Ti-binding peptide (TBP:RKLPDA) with TiO2 nanoparticles. The water peak in the NMR spectrum was selectively saturated, and the STD amplitudes for TBP were observed in the presence of TiO2, demonstrating that the side chains of the N-terminal residues Arg1 and Lys2 exhibit the strongest saturation transfer effect from water molecules; i.e., the two N-terminal residues are in contact with the TiO2 surface. The relaxation rate in the rotating frame, R1?, was observed to be high at the N-terminal residues; R1?... [Read More]
0 Replies | 20 Views
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