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• W2009814519 abstract "When pea lectin was exposed to a low pH range, it was found that the secondary structure of the lectin resisted conformational changes to a large extent up to pH 2.4 and below this pH, a sharp transition was observed which could be due to the presence of 27 acidic amino acid residues present in the protein. The effects of 1,1,1,3,3,3 hexafluoro-isopropanol (HFIP) and 2,2,2-Trifluoroethanol (TFE) on the conformation of pea lectin at pH 2.4 were studied using circular dichroism and fluorescence spectroscopy. Analysis varying the TFE concentration showed that up to 80% TFE (v/v) protein retained the residual beta-structure accompanied by a loss in tertiary structure. A similar conformation is presumed to exist at 4% HFIP (v/v), with an increase in HFIP concentration structural rearrangements occurred and a transition from beta-structure to alpha-helical structure started from 12% HFIP which completed at 30% HFIP. Our studies show the occurrence of a common intermediate in the folding pathway of pea lectin induced by two different fluoroalcohols, which differ in their mode of action to stabilize the secondary structure of a given protein. While TFE was not found to induce any alpha-helical structure, HFIP caused the transition of pea lectin, which is predominantly a beta-sheet protein, to a structure rich in alpha-helical contacts. Thus, our results also point out the possibility of a non-hierarchical model of protein folding in lectins." @default.
• W2009814519 created "2016-06-24" @default.
• W2009814519 creator A5022068766 @default.
• W2009814519 creator A5044532564 @default.
• W2009814519 date "2005-05-01" @default.
• W2009814519 modified "2023-09-24" @default.
• W2009814519 title "Characterization of a common intermediate of pea lectin in the folding pathway induced by TFE and HFIP" @default.
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• W2009814519 doi "https://doi.org/10.1016/j.bbagen.2005.02.009" @default.
• W2009814519 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15840464" @default.
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