Results 21 to 30 of about 382,475 (303)

Analysis of Hydrogen Bonds in Crystals

open access: yesCrystals, 2016
The determination of crystal structures provides important information on the geometry of species constituting crystals and on the symmetry relations between them.
Sławomir J. Grabowski
doaj   +1 more source

Ethyl 2-(2,5-dioxo-4,4-diphenylimidazolidin-1-yl)acetate

open access: yesIUCrData, 2017
The five-membered ring of the title compound, C19H18N2O4, adopts an envelope conformation. In the crystal, pairwise N—H...O hydrogen bonds form centrosymmetric dimers which are connected into chains parallel to the c-axis direction by pairwise C—H...O ...
Youssef Ramli   +5 more
doaj   +1 more source

Ethyl 4-(4-hydroxyphenyl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate monohydrate

open access: yesActa Crystallographica Section E, 2008
There are three formula units in the asymmetric unit of the title compound, C14H16N2O4·H2O. Molecules are linked by N—H...O hydrogen bonds into dimers with the common R22(8) graph-set motif.
T. N. Guru Row   +4 more
doaj   +1 more source

Syntheses and crystal structures of 2,2,5-trimethyl-1,3-dioxane-5-carboxylic acid and 2,2,5-trimethyl-1,3-dioxane-5-carboxylic anhydride

open access: yesActa Crystallographica Section E: Crystallographic Communications, 2020
In 2,2,5-trimethyl-1,3-dioxane-5-carboxylic acid, C8H14O4, the carboxyl group occupies an equatorial position on the 1,3-dioxane ring. In the crystal, O—H...O hydrogen bonds form chains of molecules, which are linked into a three-dimensional network by C—
Joseph A. Giesen   +2 more
doaj   +1 more source

Structural insights into lacto‐N‐biose I recognition by a family 32 carbohydrate‐binding module from Bifidobacterium bifidum

open access: yesFEBS Letters, EarlyView.
Bifidobacterium bifidum establishes symbiosis with infants by metabolizing lacto‐N‐biose I (LNB) from human milk oligosaccharides (HMOs). The extracellular multidomain enzyme LnbB drives this process, releasing LNB via its catalytic glycoside hydrolase family 20 (GH20) lacto‐N‐biosidase domain.
Xinzhe Zhang   +5 more
wiley   +1 more source

Crystal structure of tris(piperidinium) hydrogen sulfate sulfate

open access: yesActa Crystallographica Section E: Crystallographic Communications, 2015
In the title molecular salt, 3C5H12N+·HSO4−·SO42−, each cation adopts a chair conformation. In the crystal, the hydrogen sulfate ion is connected to the sulfate ion by a strong O—H...O hydrogen bond. The packing also features a number of N—H...O hydrogen
Tamara J. Lukianova   +2 more
doaj   +1 more source

Peptide‐based ligand antagonists block a Vibrio cholerae adhesin

open access: yesFEBS Letters, EarlyView.
The structure of a peptide‐binding domain of the Vibrio cholerae adhesin FrhA was solved by X‐ray crystallography, revealing how the inhibitory peptide AGYTD binds tightly at its Ca2+‐coordinated pocket. Structure‐guided design incorporating D‐amino acids enhanced binding affinity, providing a foundation for developing anti‐adhesion therapeutics ...
Mingyu Wang   +9 more
wiley   +1 more source

Raman Spectroscopy for the Competition of Hydrogen Bonds in Ternary (H2O–THF–DMSO) Aqueous Solutions

open access: yesMolecules, 2019
The effects of hydrogen bonds on the molecular structure of water-tetrahydrofuran (H2O−THF), water-dimethyl sulfoxide (H2O−DMSO), and water-tetrahydrofuran-dimethyl sulfoxide (H2O−THF−DMSO) in binary aqueous solutions and ternary ...
Shiliang Liu   +4 more
doaj   +1 more source

Substrate specificity of Burkholderia pseudomallei multidrug transporters is influenced by the hydrophilic patch in the substrate‐binding pocket

open access: yesFEBS Letters, EarlyView.
Multidrug transporters BpeB and BpeF from the Gram‐negative pathogen Burkholderia pseudomallei have a hydrophilic patch in their substrate‐binding pocket. Drug susceptibility tests and growth curve analyses using an Escherichia coli recombinant expression system revealed that the hydrophilic patches of BpeB and BpeF are involved in the substrate ...
Ui Okada, Satoshi Murakami
wiley   +1 more source

An upstream open reading frame regulates expression of the mitochondrial protein Slm35 and mitophagy flux

open access: yesFEBS Letters, EarlyView.
This study reveals how the mitochondrial protein Slm35 is regulated in Saccharomyces cerevisiae. The authors identify stress‐responsive DNA elements and two upstream open reading frames (uORFs) in the 5′ untranslated region of SLM35. One uORF restricts translation, and its mutation increases Slm35 protein levels and mitophagy.
Hernán Romo‐Casanueva   +5 more
wiley   +1 more source

Home - About - Disclaimer - Privacy