Das, Amlan and Sinha, Sharmistha and Acharya, Bipul R and Paul, Pinaki and Bhattacharyya, Bhabatarak and Chakrabarti, Gopal (2008) Deuterium oxide stabilizes conformation of tubulin: a biophysical and biochemical study. In: BMB Reports, 41 (1). pp. 62-67.
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The present study was aimed to elucidate the mechanism of stabilization of tubulin by deuterium oxide $(D_2O)$. Rate of decrease of tryptophan fluorescence during aging of tubulin at $4^oC$ and $37^oC$ was significantly lower in $D_2O$ than in $H_2O$. Circular dichroism spectra of tubulin after incubation at $4^oC$, suggested that complete stabilization of the secondary structure in $D_2O$ during the first 24 hours of incubation. The number of available cysteine measured by DTNB reaction was decreased to a lesser extent in $D_2O$ than in $H_2O$. During the increase in temperature of tubulin, the rate of decrease of fluorescence at 335 nm and change of CD value at 222 nm was lesser in $D_2O$. Differential Scanning calorimetric experiments showed that the $T_m$ values for tubulin unfolding in $D_2O$ were $58.6^oC$ and $62.17^oC$, and in $H_2O$ those values were $55.4^oC$ and $59.35^oC$.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Korean Society for Bipchemistry and Molecular Biology.|
|Keywords:||Circular dichroism;Deuterium oxide;Differential scanning calorimeter;Fluorescence;Protein conformational stabilization;Tubulin|
|Department/Centre:||Division of Biological Sciences > Microbiology & Cell Biology|
|Date Deposited:||11 Jul 2008|
|Last Modified:||23 Feb 2012 07:13|
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