Halogenated alcohols as solvents for proteins : FTIR spectroscopic studies

DOIResolve DOI: http://doi.org/10.1016/0167-4838(92)90141-Y
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Volume1118
Issue2
Pages139143; # of pages: 5
SubjectHalogenated alcohol; Infrared spectroscopy; Protein conformation
AbstractFourier transform infrared (FTIR) spectroscopy has been applied to investigate the secondary structure of proteins and polypeptides in halogenated alcohols. Each alcohol studied was able, as a pure liquid, to induce conversion of the β-sheet protein concanavalin A into a predominantly α-helical configuration. In 2H2O/alcohol mixtures, helicogenisis was also apparent, decreasing in the order dichloroethanol > bromoethanol > trifluoroethanol > chloroethanol > fluoroethanol. At concentrations below those found to be helicogenic, disruption of the protein secondary structure by the alcohols resulted in pronounced aggregation. At concentrations insufficient to cause noticeable disruptions of the secondary structure at room temperature, the thermal stability of the protein was greatly reduced. We suggest the helicogenic effect exhibited by halogenated alcohols to be related to a combination of a relatively low dielectric constant and a high dipole moment, the latter causing disruption of the internal hydrogen bond networks and the former causing refolding to a helical configuration. The results presented here highlight the risk of using halogenated alcohols, both as solvents for proteins and as a test of the intrinsic capacity of proteins and peptides to adopt helical secondary structures.
Publication date
PublisherElsevier Science Publishers B.V.
LanguageEnglish
AffiliationNRC Institute for Biodiagnostics; National Research Council Canada; NRC Steacie Institute for Molecular Sciences
Peer reviewedYes
NRC number47
NPARC number9148386
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Record identifier12abbeda-4b28-4f62-972c-21d6566dc2dc
Record created2009-06-25
Record modified2016-12-22
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