ChemInform Abstract: INFRARED STUDY OF ZINC OXIDE SURFACE PROPERTIES. II. HYDROGEN-CARBON MONOXIDE E INTERACTION AT ROOM TEMPERATURE

1978 ◽  
Vol 9 (16) ◽  
Author(s):  
F. BOCCUZZI ◽  
E. GARRONE ◽  
A. ZECCHINA ◽  
A. BOSSI ◽  
M. CAMIA
1965 ◽  
Vol 43 (12) ◽  
pp. 3165-3172 ◽  
Author(s):  
Ivan Haller ◽  
R. Srinivasan

The photolysis of tetramethylcyclobutan-1,3-dione was investigated in a nitrogen matrix at 4°K and in solution in cyclohexane at room temperature. Infrared spectra of the reactant after irradiation showed the formation of carbon monoxide, dimethylketene, tetramethylethylene, and a compound with an intense absorption at 1 840 cm−1 which has been identified as tetramethylcyclopropanone. Since the dimethylketene that was formed was also capable of undergoing secondary photolysis, the effect of light (mainly 2 537 Å) on dimethylketene in solution or in a nitrogen matrix, was also studied. It has been found that in solution 0.2 of the molecules of tetramethylcyclobutandione which decompose, do so to give two molecules of dimethylketene, while approximately the same number of molecules decompose to tetramethylcyclopropanone and carbon monoxide. The remainder of the molecules seem to give tetramethylethylene and carbon monoxide in a concerted process.


1987 ◽  
Vol 52 (5) ◽  
pp. 1356-1361
Author(s):  
S. Abdel Rahman ◽  
M. Elsafty ◽  
A. Hattaba

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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