Solid-state Circular Dichroism and Hydrogen Bonding, Part 2: The Case of Hypothemycin Re-investigated

Chirality ◽  
2012 ◽  
Vol 24 (9) ◽  
pp. 718-724 ◽  
Author(s):  
Gennaro Pescitelli
Keyword(s):  
Hydrogen Bonding ◽  
Circular Dichroism ◽  
Solid State ◽  
Circular Dichroïsm

Solid-state circular dichroism and hydrogen bonding: Absolute configuration of massarigenin A from Microsphaeropsis sp

Chirality ◽  
2011 ◽  
Vol 23 (8) ◽  
pp. 617-623 ◽  
Author(s):  
Hidayat Hussain ◽  
Ishtiaq Ahmed ◽  
Barbara Schulz ◽  
Siegfried Draeger ◽  
Ulrich Flörke ◽  
...  
Keyword(s):  
Hydrogen Bonding ◽  
Circular Dichroism ◽  
Solid State ◽  
Absolute Configuration ◽  
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.

scholarly journals Vibrational circular dichroism as a probe of solid‐state organisation of derivatives of cyclic β‐amino acids: Cis ‐ and trans ‐2‐aminocyclobutane‐1‐carboxylic acid

Chirality ◽  
2019 ◽  
Vol 31 (8) ◽  
pp. 547-560 ◽  
Author(s):  
Valérie Declerck ◽  
Ariel Pérez‐Mellor ◽  
Régis Guillot ◽  
David J. Aitken ◽  
Michel Mons ◽  
...  
Keyword(s):  
Amino Acids ◽  
Circular Dichroism ◽  
Solid State ◽  
Carboxylic Acid ◽  
Vibrational Circular Dichroism ◽  
Cis And Trans ◽  
Derivatives Of ◽  
Circular Dichroïsm

scholarly journals Structural Characterization of a Cyclodextrin/l-menthol Inclusion Complex in the Solid-state by Solid-state NMR and Vibrational Circular Dichroism

2020 ◽  
Vol 36 (11) ◽  
pp. 1337-1343
Author(s):  
Takahiro SAKAI ◽  
Yumiko AKAGI ◽  
Hisashi SUZUKI ◽  
Mitsuki IRIE ◽  
Tetsuya NAKAMURA ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Solid State ◽  
Inclusion Complex ◽  
Structural Characterization ◽  
Solid State Nmr ◽  
Vibrational Circular Dichroism ◽  
Circular Dichroïsm

Stereoselective interactions as manifested by vibrational circular dichroism spectra: the interplay between chiral metal complexes co-adsorbed in a montmorillonite clay

2018 ◽  
Vol 20 (39) ◽  
pp. 25421-25427 ◽  
Author(s):  
Hisako Sato ◽  
Kazuyoshi Takimoto ◽  
Hirotoshi Mori ◽  
Akihiko Yamagishi
Keyword(s):  
Circular Dichroism ◽  
Solid State ◽  
Metal Complexes ◽  
Montmorillonite Clay ◽  
Vibrational Circular Dichroism ◽  
Circular Dichroism Spectra ◽  
Circular Dichroïsm

Solid state VCD is applied for intercalated metal complexes.

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