Deuterium oxide stabilizes conformation of tubulin: A biophysical and biochemical study
| Autor: | Bipul R. Acharya, Amlan Das, Pinaki Paul, Bhabatarak Bhattacharyya, Gopal Chakrabarti, Sharmistha Sinha |
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| Předmět: |
Circular dichroism
Protein Folding DTNB Molecular Conformation Biochemistry Fluorescence Protein Structure Secondary Differential scanning calorimetry Tubulin Animals Deuterium Oxide Molecular Biology Protein secondary structure Microbiology & Cell Biology Brain Chemistry biology Calorimetry Differential Scanning Chemistry Circular Dichroism Goats Temperature General Medicine Crystallography Deuterium biology.protein Cysteine |
| Zdroj: | Scopus-Elsevier |
| Popis: | The present study was aimed to elucidate the mechanism of stabilization of tubulin by deuterium oxide (D(2)O). Rate of decrease of tryptophan fluorescence during aging of tubulin at 4 degrees C and 37 degrees C was significantly lower in D(2)O than in H(2)O. Circular dichroism spectra of tubulin after incubation at 4 degrees C, suggested that complete stabilization of the secondary structure in D(2)O during the first 24 hours of incubation. The number of available cysteine measured by DTNB reaction was decreased to a lesser extent in D(2)O than in H(2)O. 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(2)O. Differential Scanning calorimetric experiments showed that the T(m) values for tubulin unfolding in D(2)O were 58.6 degrees C and 62.17 degrees C, and in H(2)O those values were 55.4 degrees C and 59.35 degrees C. |
| Databáze: | OpenAIRE |
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