Modalities of Protein Denaturation and Nature of Denaturants

Abstract

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.

Conformationally modulated immunogenic proteins in homeopathic medicines: Does protein-based mucosal immunotherapy have the potential to treat diverse diseases?

“…Proteins can be denatured by heat, radiation, sonication, acids, alkalis, oxidizing/reducing agents etc. [58]. However, proteins are immunogenic in both native and denatured forms [29,59] and the immunogenicity of proteins is determined by their conformations (shapes) as some epitopes may be masked and some exposed when the conformations change [60].…”

“…However, proteins are immunogenic in both native and denatured forms [29,59] and the immunogenicity of proteins is determined by their conformations (shapes) as some epitopes may be masked and some exposed when the conformations change [60]. The process of denaturation/partial denaturation changes the conformation [58] and hence, the immunogenicity of the proteins.…”

INTERACTION OF METHYLENE BLUE WITH SINGLE-STRANDED POLYNUCLEOTIDES POLY(rA) AND POLY(rU) AND WITH DOUBLE_STRANDED POLYNUCLEOTIDE POLY(rA)-POLY(rU)

“…На рисунке 2 (б) приведены спектры поглощения МС (кривая 1), его комплексов с оц-poly(rA) (кривые 2-13) и МС+оц-poly(rA)+оц-poly(rU) (кривые [14][15][16][17][18]. Из приведенного рисунка видно, что спектры поглощения комплексов резко уменьшены относительно спектра поглощения МС и также сдвинуты в сторону длинных волн.…”

“…Однако, наиболее важным можно считать то, что МС проявляет терапевтические свойства к вирусам семейства коронавирусов. Недавные исследования выявили, что МС может также применяться для лечения нейродегенеративных расстройств, таких как болезнь Альцгеймера (AD), из-за его предполагаемого ингибирующего действия на агрегацию тау-белка [13][14][15][16][17][18].…”

Study of Structural Transitions of Complexes of Different Ligands With Dna and Bsa

“…One of approaches is the study of denaturation of DNA and proteins and their complexes with ligands. For revelation of molecular basis of protein denaturation, one should explain why they are divided by free-energetic barrier (which creates the transition of the type "all or nothing") [1,2]. From this point of view, denaturation of nucleic acids (NA) occurs otherwise by intermediate states, than of protein.…”