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- W2068623791 abstract "In this study we are reporting the conformational modulation as well as the plausible mechanism of structural perturbation in conalbumin (CA). The overall structure of CA is altered by the change in dielectric constant upon addition of fluoroalcohols (TFE and HFIP). We studied the formation of aggregates in CA at pH 7.0 by multiple structural probes in the presence of TFE and HFIP. The protein aggregates maximally in 15% (v/v) TFE and 3% (v/v) HFIP. ANS, ThT binding and transmission electron microscopy data suggest that the aggregates induced by TFE and HFIP have amyloid-like properties. Higher concentrations of TFE and HFIP causes increase in helical propensity. Far-UV circular dichroism, intrinsic fluorescence, ANS and ThT fluorescence data suggests that formation of a partially structured intermediate state precedes the onset of the aggregation process." @default.
- W2068623791 created "2016-06-24" @default.
- W2068623791 creator A5009106621 @default.
- W2068623791 creator A5044532564 @default.
- W2068623791 creator A5064323452 @default.
- W2068623791 date "2014-09-01" @default.
- W2068623791 modified "2023-10-18" @default.
- W2068623791 title "Fluoroalcohols-induced modulation and amyloid formation in conalbumin" @default.
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- W2068623791 doi "https://doi.org/10.1016/j.ijbiomac.2014.07.027" @default.
- W2068623791 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25062993" @default.
- W2068623791 hasPublicationYear "2014" @default.
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