Novel Means of Controlling the Solid-State Circular Dichroism Property in a Supramolecular Organic Fluorophore Comprising 4-[2-(Methylphenyl)ethynyl]benzoic Acid by Varying the Position of the Methyl Substituent

2012 ◽  
Vol 12 (4) ◽  
pp. 1859-1864 ◽  
Author(s):  
Noriaki Nishiguchi ◽  
Takafumi Kinuta ◽  
Tomohiro Sato ◽  
Yoko Nakano ◽  
Takunori Harada ◽  
...  
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.


Chirality ◽  
2011 ◽  
Vol 23 (8) ◽  
pp. 617-623 ◽  
Author(s):  
Hidayat Hussain ◽  
Ishtiaq Ahmed ◽  
Barbara Schulz ◽  
Siegfried Draeger ◽  
Ulrich Flörke ◽  
...  

2018 ◽  
Vol 20 (39) ◽  
pp. 25421-25427 ◽  
Author(s):  
Hisako Sato ◽  
Kazuyoshi Takimoto ◽  
Hirotoshi Mori ◽  
Akihiko Yamagishi

Solid state VCD is applied for intercalated metal complexes.


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