Results 21 to 30 of about 3,146,886 (266)

Crystal structure of 3-[2-(thiophen-3-yl)ethynyl]-2H-chromen-2-one

open access: yesActa Crystallographica Section E: Crystallographic Communications, 2015
In the title compound, C15H8O2S, the coumarin moiety is approximately planar (r.m.s. deviation of the 11 non-H atoms = 0.025 Å) and is slightly inclined with respect to the plane of the thiophen-3-yl ring, forming a dihedral angle of 11.75 (8)°.
Ignez Caracelli   +4 more
doaj   +1 more source

Crystal structure of dichlorido{2,6-bis[(3-phenyl-1H-pyrazol-1-yl)methyl]pyridine}cobalt(II)

open access: yesActa Crystallographica Section E: Crystallographic Communications, 2015
In the title complex, [CoCl2(C25H21N5)], the CoII atom is coordinated by two Cl atoms and two N atoms, provided by a tridentate pyrazolylpyridyl ligand, forming a slightly distorted tetrahedral geometry [range of angles: 96.51 (10) (chelate ring) to 118 ...
Kyung-sun Son   +3 more
doaj   +1 more source

Septin 9 PB domains coordinate centrosome positioning and microtubule acetylation to control epithelial polarity

open access: yesFEBS Letters, EarlyView.
Septin 9 polybasic domains couple phosphoinositide‐rich membrane binding to centrosome positioning, Golgi organization, and microtubule acetylation to control epithelial polarity. Their loss disrupts this axis, causing centrosome mispositioning, Golgi fragmentation, reduced microtubule acetylation, and polarity inversion via upregulation of the ...
Ting ting Cai   +4 more
wiley   +1 more source

Crystal structure of (4E)-4-(8-methoxy-2H-chromen-2-ylidene)-3-methyl-1-phenyl-1H-pyrazol-5(4H)-one

open access: yesActa Crystallographica Section E: Crystallographic Communications, 2015
In the title compound, C20H16N2O3, the phenyl substituent attached to the pyrazole ring makes a dihedral angle of 4.87 (7)° with the rest of the molecule.
Muhammad Salim   +4 more
doaj   +1 more source

Emerging experimental and computational methods for studying redox‐regulated structural transitions

open access: yesFEBS Letters, EarlyView.
Redox reactions can reshape proteins and alter how they behave in cells, with important consequences for health and disease. This review explores emerging experimental and computational approaches for discovering these redox‐sensitive protein switches, revealing their structural effects, and predicting their behavior, opening new opportunities to ...
Tasneem Rass   +2 more
wiley   +1 more source

Crystal structure of (2E)-1-(5-bromothiophen-2-yl)-3-(2-chlorophenyl)prop-2-en-1-one

open access: yesActa Crystallographica Section E: Crystallographic Communications, 2015
In the title compound, C13H8BrClOS, the thienyl ring is not coplanar with the benzene ring, their planes forming a dihedral angle of 13.2 (4)°. In the crystal, molecules stack along the a axis, with the interplanar separation between thienyl rings and ...
B. R. Anitha   +3 more
doaj   +1 more source

Structural and biochemical analysis of a B12 superbinder

open access: yesFEBS Letters, EarlyView.
BtuG proteins are vitamin B12 scavengers in Bacteroides thetaiotaomicron, a dominant human gut bacterium. We present crystal structures of three BtuG homologs bound to cobalamin and its precursor cobinamide, revealing picomolar binding affinities, among the highest known for any natural protein.
Jose M. Martinez Felices   +3 more
wiley   +1 more source

Ethyl 2-[(azidocarbonyl)amino]benzoate

open access: yesIUCrData, 2016
In the almost planar (r.m.s. deviation = 0.038 Å) title compound, C10H10N4O3, an intramolecular N—H...O interaction closes an S(6) ring. In the crystal, aromatic π–π stacking interactions occur [inter-centroid distance = 3.65 (2) Å].
Hasna Yassine   +4 more
doaj   +1 more source

Is π-Single Bonding (C–π–C) Possible? A Challenge in Organic Chemistry. [PDF]

open access: yes, 2023
Conferencia científicaChemical bonding systems determine the nature of molecules. In organic chemistry, there are two bonding types for carbon–carbon connections: σ-bonding and π-bonding.
Abe, Manabu
core  

The Shewanella oneidensis Fic enzyme SoFic targets the switch‐I region of EF‐Tu for AMPylation

open access: yesFEBS Letters, EarlyView.
Fic enzymes mediate diverse post‐translational modifications across all domains of life, including AMPylation. Prokaryotic EF‐Tu can be AMPylated and deAMPylated by the conserved Fic enzyme SoFic. Structural and biochemical approaches were used to characterize the effect of AMPylation on EF‐Tu, SoFic's enzymatic activities, and the enzyme‐target ...
Svenja Runge   +6 more
wiley   +1 more source

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