Cyanine Borate Penetrated Ion Pair Structures in Solution and the Solid State:  Induced Circular Dichroism

1998 ◽  
Vol 120 (8) ◽  
pp. 1705-1717 ◽  
Author(s):  
David J. Owen ◽  
Donald VanDerveer ◽  
Gary B. Schuster
Keyword(s):  
Circular Dichroism ◽  
Solid State ◽  
Ion Pair ◽  
Induced Circular Dichroism ◽  
Circular Dichroïsm

Induced circular dichroism in solid-state inclusion compounds

Chirality ◽  
2001 ◽  
Vol 13 (7) ◽  
pp. 347-350 ◽  
Author(s):  
Koichi Tanaka ◽  
Masako Kato ◽  
Fumio Toda
Keyword(s):  
Circular Dichroism ◽  
Solid State ◽  
Inclusion Compounds ◽  
Induced Circular Dichroism ◽  
Circular Dichroïsm

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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