MODELING OF THE STRUCTURE AND IR SPECTRA OF BORON DIFLUORIDE ACETYLACETONATE AND ITS HALOGEN-SUBSTITUTED DERIVATIVES

2017 ◽  
Keyword(s):  
Ir Spectra ◽  
Boron Difluoride

Modeling of the structure and IR spectra of boron difluoride acetylacetonate and its halogen-substituted derivatives

2017 ◽  
Vol 58 (6) ◽  
pp. 1079-1089 ◽  
Author(s):  
O. B. Ryabchenko ◽  
L. A. Kuarton ◽  
I. V. Svistunova ◽  
V. I. Vovna
Keyword(s):  
Ir Spectra ◽  
Boron Difluoride

Visualization of ultrasonic cavitation in visible and IR spectra

2010 ◽  
Author(s):  
A. Osterman ◽  
O. Coutier-Delgosha ◽  
M. Hocevar ◽  
B. Sirok
Keyword(s):  
Ir Spectra ◽  
Ultrasonic Cavitation

Light- or Dark-Colored, L-DOPA-Based Melanins

2018 ◽  
Author(s):  
Koen Vercruysse ◽  
Margaret M. Whalen
Keyword(s):  
Human Physiology ◽  
Ir Spectra ◽  
Immune Cells ◽  
Chemical Properties ◽  
Chemical Signature ◽  
Ft Ir

<p>This report is a continuation of previous research on the H<sub>2</sub>O<sub>2</sub>-mediated synthesis of melanin-like pigments. We synthesized and characterized L-DOPA-based pigments using air- or H<sub>2</sub>O<sub>2</sub>-mediated<sub> </sub>oxidation. We compared their physic-chemical properties and evaluated their capacity to affect the interleukin release from immune cells. The use of higher concentrations of H<sub>2</sub>O<sub>2</sub> resulted in melanin-like materials with a distinct chemical signature in their FT-IR spectra and a lighter color. All pigments enhanced the interleukin release from immune cells. The possibility that lighter-colored melanins can be generated is discussed in the context of the importance of melanin-based pigmentation in human physiology.</p>

Sulphoamidic Phtalocyaninic Pigments and Dyes(II)

2008 ◽  
Vol 59 (5) ◽  
Author(s):  
Elena Stingaciu ◽  
Corneliu Minca ◽  
Ion Sebe
Keyword(s):  
Ir Spectra ◽  
Aromatic Amines ◽  
Free Groups ◽  
Cyanuric Chloride ◽  
Layer Chromatography ◽  
Phenylene Diamine

This work concerns the synthesis of pigments and phtalocyanine dyes obtained through the sulphonation of copper phtalocyanine and amidation with some aliphatic and aromatic amines (lauryl-amine, i-propyl-amine, hexadecyl-amine, stearyl-amine and acetyl-p-phenylene-diamine) with good properties for the electrotechnic utilisation and for toner materials. The pigments with amino free groups are transformed by condensation with cyanuric chloride in phtalocyanine pigments with different tinctorial properties. The dyes were analyzed through the layer chromatography and were characterized on the IR spectra bases and tinctorial tests.

The structure and IR spectra of oxygen-containing carbofunctional trimethylgermanes

1974 ◽  
Vol 39 (9) ◽  
pp. 2651-2655 ◽  
Author(s):  
J. Pola ◽  
M. Jakoubková ◽  
V. Chvalovský
Keyword(s):  
Ir Spectra

Circular dichroism and infrared study of β-turn formation in repeat peptides of elastin

1987 ◽  
Vol 52 (5) ◽  
pp. 1356-1361
Author(s):  
S. Abdel Rahman ◽  
M. Elsafty ◽  
A. Hattaba
Keyword(s):  
Circular Dichroism ◽  
Solid State ◽  
Ir Spectra ◽  
Chain Length ◽  
Room Temperature ◽  
Infrared Study ◽  
Feature Characteristic ◽  
C 50 ◽  
The Stability ◽  
Circular Dichroïsm

The conformation of elastin-like peptides Boc-Ala-Pro-Gly-Val-APEGM, Boc-Ala-Pro-Gly-Val-Gly-Val-APEGM, Boc-Ala-Pro-Gly-Val-Ala-Pro-Gly-Val-Gly-Val-APEGM, Boc-Ala-Pro-Gly-Val-Gly-Val-Ala-Pro-Gly-Val-Gly-Val-APEGM were examined in solution using circular dichroism at 30 °C, 50 °C, and 70 °C and in solid state by IR at room temperature. The studies show that the β-turn is a significant conformational feature for peptides under investigation in solution at 30 °C and 50 °C, but at 70 °C the tetra, hexa, and decapeptides show the CD feature characteristic of the β-structure while the dodecapeptide spectra show the presence of β-turn which indicates the stability of the β-turn at this chain length. The IR spectra show that in the solid state at room temperature all investigated peptides assume essentially a β-turn except the tetrapeptide which present evidence of antiparallel β-structure. The β-turn contribution in the IR spectra increases with the increase of the chain length of the peptide.

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