Denaturation of protein is a biological phenomenon in which a protein loses its native shape due to the breaking or disruption of weak chemical bonds and interactions which makes the protein biologically inactive. It is the process where properly folded proteins formed under physiological conditions is transformed to an unfolded protein under non-physiological conditions. The process of denaturation of proteins can occur under different physiological and chemical conditions. Denaturation can be reversible or irreversible. Denaturation mostly takes places when the protein is subjected under external elements like inorganic solutes, organic solvents, acids or bases, and by heat or irradiations. The denaturing agents or denaturants widely used in protein folding or unfolding experiments are urea and guanidinium chloride (GdmCl). In denaturation, the alpha-helix structure and beta sheets structure of the native protein are disrupted and unfolds it into any random shape. We can also say that denaturation occurs due to the disruption of bonding interactions which are responsible for secondary structure and the tertiary structure of the proteins.
An equilibrium unfolding research of the recombinant zDHFR would provide information on the conformational changes of protein. In present work, the conformation of recombinant zDHFR was investigated in presence of ethanol and acetic acid. Equilibrium unfolding of recombinant zDHFR was monitored by enzymatic assay after denaturation by ethanol and acetic acid at 340 nm. Changes in secondary and tertiary structure of zDHFR with increasing ethanol and acetic acid concentrations were investigated in far-UV circular dichroism (CD) (190 to 250 nm) and fluorescence spectroscopy (emission spectra from 300 to 400 nm with an excitation wavelength of 295 nm) methods. It has been observed that in case of acetic acid-induced denaturation of zDHFR, the shift from native to denatured state occurs in a single step, whereas intermediates or non-native states are found at low concentrations of ethanol. The recent findings have significant implications for understanding how ethanol and acetic acid affect protein structure.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.