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.

Structural Differences of Ovalbumin and S-Ovalbumin Revealed by Denaturing Conditions

1997 ◽  
Vol 52 (9-10) ◽  
pp. 645-653 ◽  
Author(s):  
Corrado Paolinelli ◽  
Mario Barteri ◽  
Federico Boffi ◽  
Francesca Forastieri ◽  
Maria Cristina Gaudiano ◽  
...  
Keyword(s):  
Experimental Data ◽  
Circular Dichroism ◽  
Secondary Structure ◽  
Guanidine Hydrochloride ◽  
Stable Form ◽  
X Ray ◽  
Heat Stable ◽  
X Ray Scattering ◽  
Structural Differences ◽  
Circular Dichroïsm

We found, by circular dichroism and Raman spectroscopy measurements, that the secondary structure of the native ovalbumin and of its heat-stable form, called S-ovalbumin, is a probe of the structural differences between the two proteins. Small angle X-ray scattering and circular dichroism measurements performed on the two proteins under denaturing conditions, with different concentrations of guanidine hydrochloride, show the changes of the tertiary and secondary structure and a different pathway in the unfolding process. These experimental data confirm that the conversion of native ovalbumin into S-ovalbumin is irreversible and reveal that the response of the two proteins to the same chemical environment is different

Vibrational Circular Dichroism of Proline-Containing Oligopeptides

1996 ◽  
Vol 50 (5) ◽  
pp. 644-648 ◽  
Author(s):  
Mitsuhiro Miyazawa ◽  
Katsuhiko Inouye ◽  
Tadao Hayakawa ◽  
Yoshimasa Kyogoku ◽  
Hiromu Sugeta
Keyword(s):  
Hydrogen Bond ◽  
Circular Dichroism ◽  
Vibrational Circular Dichroism ◽  
Type Ii ◽  
Dilute Solutions ◽  
Infrared Absorption Spectra ◽  
High Concentrations ◽  
Intramolecular Hydrogen ◽  
Circular Dichroïsm ◽  
Hydrogen Bonded

Vibrational circular dichroism (VCD) and infrared absorption spectra in the amide A region of blocked oligopeptides containing proline have been obtained in apolar organic solvents in order to clarify the characteristic VCD for the intramolecularly hydrogen-bonded NH stretching involved in the turn structures of peptide chains as well as the intermolecularly hydrogen-bonded NH stretching in associated molecules. The γ-turn with the intramolecularly hydrogen-bonded C7 conformation exhibits a characteristic positive VCD band at about 3330 cm−1 in dilute solutions of Piv-Pro-NHMe and Ac-Pro-NHMe. The intramolecularly hydrogen-bonded NH stretching in the type II β-turn with C10 conformation gives rise to a positive VCD band at 3345 cm−1 for Piv-Pro-Gly-NHMe. The Gly NH group of Piv-Pro-Gly-OMe and Ac-Pro-Gly-OMe in dilute solutions assumes C7C5 conformation stabilized by a bifurcated three-center intramolecular hydrogen bond and exhibits a positive VCD band near 3300 cm−1 at a lower frequency than the intermolecularly hydrogen-bonded band. All the peptides studied give a characteristic negative—positive bisignate couplet from the high wavenumber side for the intermolecularly hydrogen-bonded NH stretching band at high concentrations.

Remarkably high solvatochromism in the circular dichroism spectra of the polyproline-II conformation: limitations or new opportunities?

2021 ◽  
Author(s):  
Vladimir Kubyshkin ◽  
Jochen Bürck ◽  
Oleg Babii ◽  
Nediljko Budisa ◽  
Anne S. Ulrich
Keyword(s):  
Circular Dichroism ◽  
Conventional Method ◽  
Secondary Structures ◽  
Circular Dichroism Spectra ◽  
Polyproline Ii ◽  
Circular Dichroïsm

Circular dichroism is a conventional method for studying the secondary structures of peptides and proteins and their transitions. While certain circular dichroism features are characteristic of α-helices and β-strands, the...

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
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