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Chemical denaturants induced folding unfolding pathway of the recombinant zebrafish dihydrofolate reductase

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Title Chemical denaturants induced folding unfolding pathway of the recombinant zebrafish dihydrofolate reductase
 
Creator Acharya, Vaishali V
Verma, Anita Kamra
Chaudhuri (Chattopadhyay), Pratima
 
Subject Denaturants
Enzymatic assay
Equilibrium unfolding
Refolding yield
UV-Visible Spectroscopy
 
Description 148-156
Denaturation of proteins plays a crucial part in cellular activities. In this study, we have investigated the folding
unfolding pathways of zebrafish dihydrofolate reductase (zDHFR) in presence of different chemical denaturants which were
found to be an influential factor for the refolding yield by UV-visible spectrophotometric analysis. The activity change of
zDHFR has been observed in presence of three different denaturants like Acetic Acid (AcOH), Sodium Dodecyl Sulphate
(SDS), and Ethanol (C2H5OH). Spectrophotometric analysis reveals that protein unfolded completely at different
concentrations and times by these denaturants. The spontaneous refolding experiments of chemically denatured zDHFR
were also conducted to verify the spontaneous refolding yield. These investigations have helped us to decipher a picture
about the denaturants contributing to achieving the refolding yield. We observed that acetic acid is a stronger denaturant
among all, and the spontaneous refolding yields were higher from SDS denaturation. In the light of the above findings,
higher spontaneous refolding yields were obtained from the low concentration of denaturants.
 
Date 2022-03-25T06:22:03Z
2022-03-25T06:22:03Z
2022-02
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://nopr.niscair.res.in/handle/123456789/59376
 
Language en
 
Publisher NIScPR-CSIR, India
 
Source IJBB Vol.59(2) [February 2022]