Copper(II) Ion-Catalyzed and Molecular Packing-Dependent Dimerization of Pyridoxal 5-Phosphate–Pyridoxamine 5-Phosphate Schiff Base as a Structural Model for in Vitro Transformation of Amino Acid by Pyridoxal 5-Phosphate: X-Ray Crystal Structural Investigation

1999 ◽  
Vol 72 (5) ◽  
pp. 947-954 ◽  
Author(s):  
Toshimasa Ishida ◽  
Reijirou Manabe ◽  
Yasuko In ◽  
Hajime Takashima ◽  
Kunihiro Kitamura ◽  
...  
Keyword(s):  
Schiff Base ◽  
Amino Acid ◽  
Structural Investigation ◽  
Structural Model ◽  
Molecular Packing ◽  
X Ray ◽  
In Vitro Transformation ◽  
Crystal Structural

Synthesis, Characterization and X-Ray Crystal Structure of the New Schiff Base and Anticandidal Evaluation

2019 ◽  
Vol 41 (6) ◽  
pp. 1090-1090
Author(s):  
Mehmet Poyraz Mehmet Poyraz ◽  
Musa Sari Musa Sari ◽  
Halil Berber Halil Berber ◽  
Nursenem Karaca and Fatih Demirci Nursenem Karaca and Fatih Demirci
Keyword(s):  
Schiff Base ◽  
Spectroscopic Techniques ◽  
X Ray Diffraction ◽  
X Ray ◽  
Microdilution Method ◽  
Broth Microdilution Method ◽  
Ft Ir ◽  
Anticandidal Activity ◽  
Crystal Structural

A new Schiff base, namely 2-methoxy-6-((2-(4 nitrophenyl) hydrazineylidene) methyl)phenol was synthesized and characterized by melting points, elemental analysis, thermogravimetric analysis and spectroscopic techniques (FT-IR, 1H-NMR and UV-VIS spectra). The chemical structure of compound was further confirmed by single crystal structural X-ray diffraction. The Schiff base is crystallized in the triclinic space group P-1. In the crystal, molecules are linked by O-H…O hydrogen bonds between the hydroxy “-O-” atom and the methoxy “-O-” atom. Furthermore, the synthesized Schiff base was tested for the in vitro anticandidal activities using CLSI broth microdilution method against human pathogenic Candida albicans, C. parapsilosis and C. krusei standard strains. In the anticandidal activity test results, the new Schiff base was found to be effective at 1 mg/mL - 0.25 mg/mL concentrations. (The last line omitted) (The sentence marked in red will be deleted)

Electron probe x-ray microanalysis and electron microscopy of amino acid absorption and transport by the small intestine: inhibition by chemical poisons and correlation to the elemental composition of the epithelial cells

1986 ◽  
Vol 44 ◽  
pp. 134-135
Author(s):  
A. J. Tousimis
Keyword(s):  
Small Intestine ◽  
Amino Acid ◽  
Epithelial Cells ◽  
Elemental Composition ◽  
Isotope Labeling ◽  
Structural Components ◽  
X Ray ◽  
Human Small Intestine ◽  
Transport Studies

The elemental composition of amino acids is similar to that of the major structural components of the epithelial cells of the small intestine and other tissues. Therefore, their subcellular localization and concentration measurements are not possible by x-ray microanalysis. Radioactive isotope labeling: I131-tyrosine, Se75-methionine and S35-methionine have been successfully employed in numerous absorption and transport studies. The latter two have been utilized both in vitro and vivo, with similar results in the hamster and human small intestine. Non-radioactive Selenomethionine, since its absorption/transport behavior is assumed to be the same as that of Se75- methionine and S75-methionine could serve as a compound tracer for this amino acid.

X-Ray Structural Investigation of the Chiral Recognition of Brucine in Salt Formation with an N-Protected Amino Acid,N-Phthaloyl-threo-β-hydroxy-D- and L-leucine

1993 ◽  
Vol 66 (5) ◽  
pp. 1501-1510 ◽  
Author(s):  
Shigeru Kuwata ◽  
Jumpei Tanaka ◽  
Norihiro Onda ◽  
Takashi Yamada ◽  
Toshifumi Miyazawa ◽  
...  
Keyword(s):  
Amino Acid ◽  
Chiral Recognition ◽  
Structural Investigation ◽  
Salt Formation ◽  
X Ray ◽  
Protected Amino Acid

scholarly journals Co-crystal structure of the iMango-III fluorescent RNA aptamer using an X-ray free-electron laser

2019 ◽  
Vol 75 (8) ◽  
pp. 547-551 ◽  
Author(s):  
Robert J. Trachman ◽  
Jason R. Stagno ◽  
Chelsie Conrad ◽  
Christopher P. Jones ◽  
Pontus Fischer ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Single Crystal ◽  
Free Electron ◽  
Free Electron Laser ◽  
Structural Model ◽  
Data Sets ◽  
Data Set ◽  
X Ray ◽  
Turn On

Turn-on aptamers are in vitro-selected RNAs that bind to conditionally fluorescent small molecules and enhance their fluorescence. Upon binding TO1-biotin, the iMango-III aptamer achieves the largest fluorescence enhancement reported for turn-on aptamers (over 5000-fold). This aptamer was generated by structure-guided engineering and functional reselection of the parental aptamer Mango-III. Structures of both Mango-III and iMango-III have previously been determined by conventional cryocrystallography using synchrotron X-radiation. Using an X-ray free-electron laser (XFEL), the room-temperature iMango-III–TO1-biotin co-crystal structure has now been determined at 3.0 Å resolution. This structural model, which was refined against a data set of ∼1300 diffraction images (each from a single crystal), is largely consistent with the structures determined from single-crystal data sets collected at 100 K. This constitutes a technical benchmark on the way to XFEL pump–probe experiments on fluorescent RNA–small molecule complexes.

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