scholarly journals Conformational Transitions in Poly{n-hexyl-[(S)-3-methylpentyl]silylene} in Dilute Solution:  Temperature and Molecular Weight Dependence Detected by Circular Dichroism‡

2001 ◽  
Vol 34 (18) ◽  
pp. 6519-6525 ◽  
Author(s):  
Ken Terao ◽  
Yoshimi Terao ◽  
Akio Teramoto ◽  
Naotake Nakamura ◽  
Michiya Fujiki ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Circular Dichroism ◽  
Conformational Transitions ◽  
Solution Temperature ◽  
Dilute Solution ◽  
Molecular Weight Dependence ◽  
Circular Dichroïsm

Water-soluble lysine-containing polypeptides. IV. The synthesis, characterization,and circular dichroism spectra of sequential polypeptides formed from dipeptides of lysine and amino acids of increasing side chain size

1977 ◽  
Vol 55 (24) ◽  
pp. 4257-4266 ◽  
Author(s):  
Lewis A. Slotin ◽  
Denis R. Lauren ◽  
Ross E. Williams
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Circular Dichroism ◽  
Secondary Structure ◽  
Gel Filtration ◽  
Circular Dichroism Spectroscopy ◽  
Water Soluble ◽  
Side Chain ◽  
Circular Dichroism Spectra ◽  
Circular Dichroïsm

Several polypeptides have been synthesized which contain the alternating sequence lysyl-X, where X = gly, L-ala, D-ala, L-val, L-leu, and L-phe. The polypeptides have been characterized by gel filtration (molecular weight) and by circular dichroism spectroscopy (secondary structure).

scholarly journals Structural determinants in a library of low molecular weight gelators

Soft Matter ◽  
2015 ◽  
Vol 11 (6) ◽  
pp. 1174-1181 ◽  
Author(s):  
Kyle L. Morris ◽  
Lin Chen ◽  
Alison Rodger ◽  
Dave J. Adams ◽  
Louise C. Serpell
Keyword(s):  
Electron Microscopy ◽  
Molecular Weight ◽  
Circular Dichroism ◽  
Low Molecular Weight ◽  
Combined Approach ◽  
Structural Determinants ◽  
X Ray ◽  
Fibre Diffraction ◽  
Low Molecular Weight Gelators ◽  
Circular Dichroïsm

The structures of hydrogels formed by naphthalene dipeptide library were explored using a combined approach of electron microscopy, X-ray fibre diffraction and circular dichroism.

Conformational Transitions of Ferricytochrome c in Strong Inorganic Acids

2006 ◽  
Vol 71 (11-12) ◽  
pp. 1627-1641 ◽  
Author(s):  
Marek Stupák ◽  
Jaroslava Bágeľová ◽  
Diana Fedunová ◽  
Marián Antalík
Keyword(s):  
Circular Dichroism ◽  
High Spin ◽  
Low Temperatures ◽  
Magnetic Circular Dichroism ◽  
High Spin State ◽  
Conformational Transitions ◽  
Optical Absorption Spectroscopy ◽  
Spin States ◽  
Inorganic Acids ◽  
Circular Dichroïsm

Conformational transitions of horse heart ferricytochrome c (ferricyt c) have been investigated in the presence of strong inorganic acids and their salts by optical absorption spectroscopy, magnetic circular dichroism and circular dichroism. In the presence of acids (HClO4 or H2SO4, pH 2) or their salts (1 M NaClO4 or Na2SO4, pH 2, 25 °C), the three ligation states of ferricyt c heme were identified. One is the high-spin state: His18-Fe-H2O (40-50%), and two are the low-spin states: His18-Fe-Met80 (30-25%) and His18-Fe-His (30-25%). Under these conditions low temperatures facilitate native heme coordination of ferricyt c. Transition from low-spin to high-spin heme coordination of ferricyt c is complete in 1 M HClO4 or 3 M H2SO4. At the concentration of HClO4 and H2SO4 above 3 M, different behavior in spectral transitions of ferricyt c near the heme is observed. High-spin pentacoordinated ferricyt c with the heme ligand of His18-Fe is formed in 8 M H2SO4. This state is unstable at higher concentration of H2SO4 and porphyrin ferricyt c is formed. At HClO4 concentration higher than 3 M, the new, until this time not observed heme coordination structure of ferricyt c originates.

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