Circular Dichroism of Oriented Helical Polypeptides: the Alpha‐Helix

1972 ◽  
Vol 57 (8) ◽  
pp. 3469-3477 ◽  
Author(s):  
Richard Mandel ◽  
G. Holzwarth
Keyword(s):  
Circular Dichroism ◽  
Alpha Helix ◽  
Circular Dichroïsm

scholarly journals Protein conformation of potato (Solanum tuberosum) lectin determined by circular dichroism

1986 ◽  
Vol 233 (3) ◽  
pp. 731-736 ◽  
Author(s):  
G J van Holst ◽  
S R Martin ◽  
A K Allen ◽  
D Ashford ◽  
N N Desai ◽  
...  
Keyword(s):  
Solanum Tuberosum ◽  
Circular Dichroism ◽  
Protein Conformation ◽  
Alpha Helix ◽  
Type Ii ◽  
Beta Turn ◽  
Heat Stable ◽  
Polyproline Ii ◽  
Disulphide Bonds ◽  
Circular Dichroïsm

The structure of potato (Solanum tuberosum) lectin, which is a hydroxyproline-rich glycoprotein, has been investigated by circular dichroism. The spectra of the native lectin, and of the oxidized, reduced and carboxymethylated and deglycosylated derivatives were examined, as was a hydroxyproline-rich glycopeptide and its deglycosylated derivative. It is concluded that the lectin contains about 35% polyproline II conformation, 34% type II beta-turn and 31% irregular conformation. No indications were found for the presence of alpha-helix or beta-sheet conformations. The polyproline II conformation is heat-stable, but is markedly destabilized by deglycosylation. The type II beta-turn is destabilized by cleavage of disulphide bonds.

scholarly journals A circular-dichroism study of epidermolytic toxins A and B from Staphylococcus aureus

1982 ◽  
Vol 203 (3) ◽  
pp. 775-778 ◽  
Author(s):  
C J Bailey ◽  
S R Martin ◽  
P M Bayley
Keyword(s):  
Staphylococcus Aureus ◽  
Circular Dichroism ◽  
Alpha Helix ◽  
Side Chain ◽  
Initial Increase ◽  
Beta Sheet ◽  
Circular Dichroism Spectra ◽  
Aromatic Side Chain ◽  
Circular Dichroïsm

The far-u.v. circular-dichroism spectra of the two epidermolytic toxins was analysed into fractional contributions of 0.09 helix and 0.46 beta-sheet to each toxin structure. Trifluoroethanol perturbation caused an initial increase in dichroic absorption at 205 nm and then a change characterized as a beta-sheet-to-alpha-helix transition. The intense near-u.v. spectra suggested that the toxins have unusually rigid, though different, aromatic-side-chain arrangements.

Characterization of Tamm-Horsfall Urinary Glycoprotein

1973 ◽  
Vol 31 ◽  
pp. 420-421
Author(s):  
John P. Robinson ◽  
J. David Puett
Keyword(s):  
Electron Microscopy ◽  
Circular Dichroism ◽  
Secondary Structure ◽  
Quaternary Structure ◽  
Normal Adult ◽  
Morphological Properties ◽  
Adult Males ◽  
Circular Dichroïsm ◽  
Urinary Glycoprotein

Much work has been reported on the chemical, physical and morphological properties of urinary Tamm-Horsfall glycoprotein (THG). Although it was once reported that cystic fibrotic (CF) individuals had a defective THG, more recent data indicate that THG and CF-THG are similar if not identical.No studies on the conformational aspects have been reported on this glycoprotein using circular dichroism (CD). We examined the secondary structure of THG and derivatives under various conditions and have correlated these results with quaternary structure using electron microscopy.THG was prepared from normal adult males and CF-THG from a 16-year old CF female by the method of Tamm and Horsfall. CF female by the method of Tamm and Horsfall.

Circular dichroism spectra of adsorbed dye-aggregates

1968 ◽  
Vol 65 ◽  
pp. 146-151 ◽  
Author(s):  
G. Scheibe ◽  
O. Wörz ◽  
F. Haimerl ◽  
W. Seiffert ◽  
J. Winkler
Keyword(s):  
Circular Dichroism ◽  
Circular Dichroism Spectra ◽  
Circular Dichroïsm
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