Piper methysticum Forst
Soluble in Chloroform,Dichloromethane,Ethyl Acetate,DMSO,Acetone,etc.
493.0±45.0 °C at 760 mmHg
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provides coniferyl ferulate(CAS#:39986-86-2) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate
Members of the ATP-binding cassette superfamily couple the energy from ATP hydrolysis to the active transport of substrates across the membrane. The maltose transporter, a well characterized model system, consists of a periplasmic maltose-binding protein (MBP) and a multisubunit membrane transporter, MalFGK2. On the basis of the structure of the MBP-MalFGK2 complex in an outward-facing conformation (Oldham, M. L., Khare, D., Quiocho, F. A., Davidson, A. L., and Chen, J. (2007) Nature 450, 515-521), we identified two mutants in transmembrane domains MalF and MalG that generated futile cycling; although interaction with MBP stimulated the ATPase activity of the transporter, maltose was not transported. Both mutants appeared to disrupt the normal transfer of maltose from MBP to MalFGK2. In the first case, substitution of aspartate for glycine in the maltose-binding site of MalF likely generated a futile cycle by preventing maltose from binding to MalFGK2 during the catalytic cycle. In the second case, a four-residue deletion of a periplasmic loop of MalG limited its reach into the maltose-binding pocket of MBP, allowing maltose to remain associated with MBP during the catalytic cycle. Retention of maltose in the MBP binding site in the deletion mutant, as well as insertion of this loop into the binding site in the wild type, was detected by EPR as a change in mobility of a nitroxide spin label positioned near the maltose-binding pocket of MBP.
ABC Transporter, Carbohydrate-binding Protein, Electron Paramagnetic Resonance (EPR), Membrane Proteins, Protein Conformation, Uncoupling
Uncoupling Substrate Transport from ATP Hydrolysis in the Escherichia coli Maltose Transporter*An external file that holds a picture, illustration, etc. Object name is sbox.jpg
Jinming Cui崔 金明, Sabiha Qasim, and Amy L. Davidson1
2010 Dec 17
The basis of cross‐suppression between rod and cone channels has long been an enigma. Using rabbit retinal connectome RC1, we show that all cone bipolar cell (BC) classes inhibit rod BCs via amacrine cell (AC) motifs (C1-6); that all cone BC classes are themselves inhibited by AC motifs (R1-5, R25) driven by rod BCs. A sparse symmetric AC motif (CR) is presynaptic and postsynaptic to both rod and cone BCs. ON cone BCs of all classes drive inhibition of rod BCs via motif C1 wide‐field GABAergic ACs (γACs) and motif C2 narrow field glycinergic ON ACs (GACs). Each rod BC receives ≈10 crossover AC synapses and each ON cone BC can target ≈10 or more rod BCs via separate AC processes. OFF cone BCs mediate monosynaptic inhibition of rod BCs via motif C3 driven by OFF γACs and GACs and disynaptic inhibition via motifs C4 and C5 driven by OFF wide‐field γACs and narrow‐field GACs, respectively. Motifs C4 and C5 form halos of 60-100 inhibitory synapses on proximal dendrites of AI γACs. Rod BCs inhibit surrounding arrays of cone BCs through AII GAC networks that access ON and OFF cone BC patches via motifs R1, R2, R4, R5 and a unique ON AC motif R3 that collects rod BC inputs and targets ON cone BCs. Crossover synapses for motifs C1, C4, C5, and R3 are 3-4× larger than typical feedback synapses, which may be a signature for synaptic winner‐take‐all switches. J. Comp. Neurol. 527:87-116, 2019. © 2016 The Authors The Journal of Comparative Neurology Published by Wiley Periodicals, Inc.
amacrine cells, synapses, networks, retina, transmission electron microscopy, RRID AB_2341093, RRID AB_2532053, RRID AB_2532055, RRID AB_2532057, RRID AB_2532059, RRID AB_2532060, RRID AB_2532061, RRID SCR‐002937, RRID SCR‐008606, RRID SCR_008394, RRID SCR_001622, RRID SCR_005986, rod vision, cone vision, connectomics
Rod‐cone crossover connectome of mammalian bipolar cells
J. Scott Lauritzen, 1 Crystal L. Sigulinsky, 2 James R. Anderson, 2 Michael Kalloniatis, 3 Noah T. Nelson, 2 Daniel P. Emrich, 2 Christopher Rapp, 2 Nicholas McCarthy, 2 Ethan Kerzner, 4 Miriah Meyer, 4 Bryan W. Jones, 2 and Robert E. Marccorresponding author 2
2019 Jan 1;
Phase inhomogeneity of otherwise chemically homogenous electronic systems is an essential ingredient leading to fascinating functional properties, such as high-Tc superconductivity in cuprates, colossal magnetoresistance in manganites and giant electrostriction in relaxors. In these materials distinct phases compete and can coexist owing to intertwined ordered parameters. Charge degrees of freedom play a fundamental role, although phase-separated ground states have been envisioned theoretically also for pure spin systems with geometrical frustration that serves as a source of phase competition. Here we report a paradigmatic magnetostructurally inhomogenous ground state of the geometrically frustrated α-NaMnO2 that stems from the system’s aspiration to remove magnetic degeneracy and is possible only due to the existence of near-degenerate crystal structures. Synchrotron X-ray diffraction, nuclear magnetic resonance and muon spin relaxation show that the spin configuration of a monoclinic phase is disrupted by magnetically short-range-ordered nanoscale triclinic regions, thus revealing a novel complex state of matter.
Frustration-induced nanometre-scale inhomogeneity in a triangular antiferromagnet
A. Zorko,a,1,2 O. Adamopoulos,3 M. Komelj,1 D. Arcon,1,4 and A. Lappas3
2014 Jan 29