Chiral Sulfur Compounds. XVIII. Structure and Conformation of Methyl (E,S*)-3-Phenyl-2-(phenylsulfinyl)propenoate

1992 ◽  
Vol 45 (11) ◽  
pp. 1923 ◽  
Author(s):  
KA Hellmund ◽  
SG Pyne ◽  
BW Skelton ◽  
AH White
Keyword(s):  
Circular Dichroism ◽  
Solid State ◽  
Structural Analysis ◽  
Title Compound ◽  
Sulfur Compounds ◽  
Methanol Solution ◽  
X Ray ◽  
Circular Dichroïsm

The X-ray structural analysis of the title compound shows that the s-cis conformation is favoured in the solid state. This conformation is consistent with circular dichroism studies in methanol solution.

Chiral Sulfur Compounds. XX. Solid-State Structures and Conformations of (E) Vinyl Sulfoximines

1993 ◽  
Vol 46 (1) ◽  
pp. 143 ◽  
Author(s):  
ZM Dong ◽  
SG Pyne ◽  
BW Skelton ◽  
AH White
Keyword(s):  
Solid State ◽  
Structural Analysis ◽  
Sulfur Compounds ◽  
X Ray ◽  
Solid State Structures

The X-ray structural analysis of (E)-S-phenyl-S-(2-phenylethenyl)-N-(p- tolylsulfonyl ) sulfoximine and (E)-N-methyl-S-phenyl-S-(2-phenylethenyl) sulfoximine shows that the s- cis conformation, in which the C=C and S=O bonds are approximately syn coplanar, is favoured in the solid state.

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.

scholarly journals Soft x-ray absorption spectroscopy and magnetic circular dichroism as operando probes of complex oxide electrolyte gate transistors

2020 ◽  
Vol 116 (20) ◽  
pp. 201905
Author(s):  
Biqiong Yu ◽  
Guichuan Yu ◽  
Jeff Walter ◽  
Vipul Chaturvedi ◽  
Joseph Gotchnik ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Absorption Spectroscopy ◽  
Magnetic Circular Dichroism ◽  
Complex Oxide ◽  
X Ray ◽  
X Ray Absorption ◽  
Circular Dichroïsm ◽  
Oxide Electrolyte
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