Infrared study of the lambda transition and molecular configuration in crystalline ferrocene

1973 ◽  
Vol 59 (6) ◽  
pp. 3027-3030 ◽  
Author(s):  
I. J. Hyams ◽  
Arza Ron
Keyword(s):  
Molecular Configuration ◽  
Infrared Study ◽  
Lambda Transition

Far infrared study of the giant star forming complex W 51

2002 ◽  
Vol 4 ◽  
pp. 333-333
Author(s):  
S. K. Ghosh ◽  
D. K. Ojha ◽  
R. P. Verma
Keyword(s):  
Far Infrared ◽  
Infrared Study ◽  
Giant Star ◽  
Star Forming

In infrared study of sulphated ZrO2-TiO2 mixed oxides

2005 ◽  
Vol 30 (1) ◽  
pp. 49-54 ◽  
Author(s):  
Abdelaziz Sahibed-Dine ◽  
Mhamed Sadiq ◽  
Naima Aderdour ◽  
Mohamed Bensitel
Keyword(s):  
Mixed Oxides ◽  
Infrared Study

An Infrared Study Using a Scaled Model.

1995 ◽  
Author(s):  
Lou Massa ◽  
Peter O. Cervenka
Keyword(s):  
Scaled Model ◽  
Infrared Study

Infrared study of pyridine oxidation on Fe-Mo-O catalyst

1972 ◽  
Vol 37 (6) ◽  
pp. 1975-1977 ◽  
Author(s):  
L. Kubelková ◽  
P. Jírů
Keyword(s):  
Infrared Study

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.

A Near‐Infrared Study of the NS 14 Bipolar Nebula

1998 ◽  
Vol 509 (2) ◽  
pp. 749-760 ◽  
Author(s):  
Eric M. Howard ◽  
Judith L. Pipher ◽  
William J. Forrest
Keyword(s):  
Near Infrared ◽  
Infrared Study
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