Trifluoroethanol stabilizes the pH 4 folding intermediate of sperm whale apomyoglobin

Journal of Molecular Biology
Y Luo, R L Baldwin

Abstract

2,2,2-Trifluoroethanol (TFE) is known to stabilize peptide helices by strengthening hydrogen bonds. On the other hand, TFE destabilizes native proteins, as we confirm here, presumably by weakening the hydrophobic interaction. The stability of the pH 4 folding intermediate of apomyoglobin is known to depend both on the strength of the individual A, G, and H helices and on hydrophobic interactions between helices. We ask which effect of TFE dominates in this case: strengthening helices or weakening hydrophobic interactions between helices? Protein stability is measured by denaturant-induced unfolding curves, and two-state unfolding is tested by monitoring both far-UV CD and tryptophan fluorescence emission. Low concentrations of TFE strongly stabilize the pH 4 folding intermediate. Moreover, low concentrations of TFE compensate for helix-destabilizing mutations in the A and G helices. Consequently, enhancing helix propensity, rather than weakening the hydrophobic interaction, is the dominant effect of TFE on the folding intermediate. This result agrees with earlier mutational evidence that helix propensities are very important in determining the stability of the pH 4 intermediate. Although TFE destabilizes native holomyoglobin, a...Continue Reading

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Citations

Aug 1, 2014·PloS One·Mariela P MezzinaM Julia Pettinari
Aug 18, 2004·Proceedings of the National Academy of Sciences of the United States of America·Angela M Bertagna, Doug Barrick
Sep 10, 2004·Biopolymers·Ana Sofia L CarvalhoEduardo Pinho e Melo
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Jan 22, 2015·Proteomics·Helen S BeestonAlison E Ashcroft
May 28, 2009·IUBMB Life·Yan FuYongzhang Luo
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May 7, 2002·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·Hong-Wei ZhouHai-Meng Zhou
Apr 26, 2002·The Journal of Biological Chemistry·Sunggoo YunHee Cheon Lee
May 3, 2019·Journal of Biomolecular Structure & Dynamics·Tristan RichardGrégory Da Costa
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