Effect of Guanidine Hydrochloride on Circular Dichroism of Yeast tRNA

1972 ◽  
Vol 71 (6) ◽  
pp. 1069-1071
Author(s):  
Nobuo OKABE ◽  
Keiko SUYARI ◽  
Ken-ichi TOMITA
Keyword(s):  
Circular Dichroism ◽  
Guanidine Hydrochloride ◽  
Yeast Trna ◽  
Circular Dichroïsm

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

scholarly journals Sodium chloride-induced conformational change in tRNA as measured by circular dichroism

2015 ◽  
Vol 38 (1) ◽  
pp. 1-5
Author(s):  
Szymon Sarbak ◽  
Melania Kujawa ◽  
Hanna Jurga-Nowak ◽  
Andrzej Dobek
Keyword(s):  
Circular Dichroism ◽  
Sodium Chloride ◽  
Strong Relationship ◽  
Sodium Ions ◽  
Stabilization Process ◽  
Yeast Trna ◽  
Trna Structure ◽  
Significant Difference ◽  
Circular Dichroïsm ◽  
Chloride Concentrations

Abstract The effect of 0.01-1 M sodium ions on the conformation of the folded brewer’s yeast tRNAPhe was examined by circular dichroism method in the region 200-350 nm. The minimum peak at about 210 nm for tRNA solution with 50 mM sodium chloride showed a decrease in magnitude by 26-30% in comparison to that recorded for the solution of higher NaCl content. The depths of the peaks at 225 nm and 233 nm for two solutions with the lowest sodium chloride concentrations (cNaCl = 10mM, cNaCl = 50mM) were changed by 3-10% relative to the those in the spectra of other samples, for the 260 nm maximum peak a decrease in height was 21-25%. In the region 300-350 nm no significant difference was observed. The results point to a strong relationship between concentration of sodium ions and stabilization process of secondary and tertiary tRNA structure, which indicates the influence of sodium ions on stacking and base-pairing interactions.

scholarly journals Folding mechanism of canine milk lysozyme studied by circular dichroism and fluorescence spectroscopy

2003 ◽  
Vol 17 (2-3) ◽  
pp. 183-193 ◽  
Author(s):  
Masaharu Nakao ◽  
Munehito Arai ◽  
Takumi Koshiba ◽  
Katsutoshi Nitta ◽  
Kunihiro Kuwajima
Keyword(s):  
Circular Dichroism ◽  
Fluorescence Spectroscopy ◽  
Molten Globule ◽  
Guanidine Hydrochloride ◽  
Folding Intermediates ◽  
Equilibrium Unfolding ◽  
Burst Phase ◽  
The Relationship ◽  
Kinetics Of ◽  
Circular Dichroïsm

We have studied the guanidine hydrochloride‒induced equilibrium unfolding and the kinetics of refolding of canine milk lysozyme by circular dichroism and fluorescence spectroscopy. The thermodynamic analysis of the equilibrium unfolding measured by circular dichroism and fluorescence has shown that unfolding is represented by a three‒state mechanism and that the intermediate state of canine milk lysozyme is remarkably more stable than the intermediates observed in other lysozyme and α-lactalbumin. In the kinetic refolding of this protein, there are at least two kinetic intermediates; a burst=phase intermediate accumulated within the dead time (4 ms) of the measurement and an intermediate that has been observed during the kinetics with a rate constant of 10–20 s–1after the burst phase. This result is apparently in contrast with those previously observed in the kinetic refolding of α‒lactalbumin and equine lysozyme that show only the burst‒phase intermediate. The relationship between the extraordinarily stable equilibrium molten globule and the kinetic folding intermediates will be discussed.

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