Open AccessModalities of Protein Denaturation and Nature of Denaturants
Author(s) -
Vaishali V. Acharya,
Pratima Chaudhuri
Publication year - 2021
Publication title -
international journal of pharmaceutical sciences review and research
Language(s) - English
Resource type - Journals
ISSN - 0976-044X
DOI - 10.47583/ijpsrr.2021.v69i02.002
Subject(s) - denaturation (fissile materials) , guanidinium chloride , chemistry , protein folding , biophysics , protein secondary structure , protein structure , urea , crystallography , folding (dsp implementation) , protein tertiary structure , helix (gastropod) , biochemistry , biology , enzyme , ecology , nuclear chemistry , snail , electrical engineering , engineering
Denaturation of protein is a biological phenomenon in which a protein loses its native shape due to the breaking or disruption ofweak chemical bonds and interactions which makes the protein biologically inactive. It is the process where properly folded proteinsformed 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 orirreversible. Denaturation mostly takes places when the protein is subjected under external elements like inorganic solutes, organicsolvents, acids or bases, and by heat or irradiations. The denaturing agents or denaturants widely used in protein folding or unfoldingexperiments 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.