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Comparison of the effects of 2,2,2-trifluoroethanol on peptide and protein structure and function

Povey, Jane F., Smales, Christopher Mark, Hassard, S.J., Howard, Mark J. (2007) Comparison of the effects of 2,2,2-trifluoroethanol on peptide and protein structure and function. Journal of Structural Biology, 157 (2). pp. 329-338. ISSN 1047-8477. (doi:10.1016/j.jsb.2006.07.008) (Access to this publication is currently restricted. You may be able to access a copy if URLs are provided) (KAR id:36)

Language: English

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The co-solvent 2,2,2-trifluoroethanol (TFE) has been often used to aid formation of secondary structure in solution peptides or alternately as a denaturant within protein folding studies. Hen egg white lysozyme (HEWL) and a synthetic model peptide defining HEWL helix-4 were used as comparative model systems to systematically investigate the effect of increasing TFE concentrations on the structure of proteins and peptides. HEWL was analyzed using NMR, far-UV CD and fluorescence spectroscopy; with correlation of these results towards changes in enzymatic activity and the helix-4 peptide was analysed using NMR. Data illustrates two conflicting modes of interaction: Low TFE concentrations stabilize tertiary structure, observed from an increase in the number of NMR NOE contacts. Higher TFE concentrations denatured HEWL with the loss of lysozyme tertiary structure. The effects of TFE upon secondary structural elements within HEWL are distinct from those observed for the helix-4 peptide. This illustrates a dissimilar interaction of TFE towards both protein and peptide at equivalent TFE concentrations. The concentration that TFE promotes stabilization over denaturation is likely to be protein dependent although the structural action can be extrapolated to other protein systems with implications for the use of TFE in structural stability studies.

Item Type: Article
DOI/Identification number: 10.1016/j.jsb.2006.07.008
Uncontrolled keywords: 2,2,2-trifluoroethanol (TFE); hen egg white lysozyme; enzymatic activity; NMR; protein folding
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Mark Smales
Date Deposited: 19 Dec 2007 17:47 UTC
Last Modified: 16 Nov 2021 09:38 UTC
Resource URI: (The current URI for this page, for reference purposes)
Smales, Christopher Mark:
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