Predicted and trifluoroethanol-induced α-helicity of polypeptides

Analysis of the architecture of the transcription factor σN (σ54) and its domains by circular dichroism

“…It was poorly soluble and analysed only in an SDS (data not shown) or a trifluoroethanol (TFE) solution. TFE is a known ␣-helix inducer (see, for example, Luidens et al, 1996), so the observed 27% ␣-helical content for this peptide is likely to be an extreme upper limit. Measurements in lower TFE support this view ( Table 1).…”

Assemblages of prion fragments: novel model systems for understanding amyloid toxicity

“…Conformational analyses of the above two peptides in structure-forming solvents such as 2,2,2-trifluoroethanol (TFE) were carried out to study the intrinsic helix-forming propensity of these peptides. TFE has been used extensively by various workers to enhance the helical propensity of peptides (Luidens et al, 1996;Bodkin and Goodfellow, 1996;Jasanoff and Fersht, 1994). We observed both PrP(119-126) and PrP(121-127) form fibrils on aging in aqueous solution.…”

Solution structure of the Equine Infectious Anemia Virus p9 protein: a rationalization of its different ALIX binding requirements compared to the analogous HIV-p6 protein

“…We simulated a hydrophobic environment by using the organic solvent trifluoroethanol (TFE) to assess the degree of secondary structure under hydrophobic conditions. TFE is chosen for its well known characteristics as it favors intramolecular interactions and stabilizes secondary structure, particularly α-helices in domains of a peptide that have a propensity for such secondary structure [18]. As TFE tends to disrupt quaternary structure and dissociate peptide aggregates, it can alleviate problems occurring with intermolecular interactions in the higher concentration ranges required for NMR investigations and provide a platform to perform CD and NMR studies under similar solution conditions.…”