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Additional Supporting Information may be found in the online version of this article.

FilenameFormatSizeDescription
pro2338-sup-0001-suppinfo.docx26KSupporting Information
pro2338-sup-0002-suppFig1.tif30KFigure S1. Fluorescence spectra for Y79F under different GdnHCl concentration. The concentration of GdnHCl from a to g is 0, 0.5, 1.2, 1.5, 1.8, 2.0, 2.5 M, respectively.
pro2338-sup-0003-suppFig2.tif49KFigure S2. Urea induced unfolding of Y79W (●). Data are fitted by using eq. (9).
pro2338-sup-0004-suppFig3.tif50KFigure S3. Urea induced unfolding of Y79WW83F (●). Data are fitted by using eq. (9).
pro2338-sup-0005-suppFig4.tif49KFigure S4. GdnHCl induced unfolding of Y79WW83F (●). Data are fitted by using eq. (9).
pro2338-sup-0006-suppFig5.tif380KFigure S5 A. Segment of apoCopC encompassing residues 69–81 of strands 5 and 6. The hydrogen bond between the hydroxyl group of Tyr79 and the backbone carbonyl group of Thr75 (the tyrosine corner) is shown (PDB: 1M42). B. Comparison of apoCopC (Tyr79 in green) and Y79F (Phe79 in cyan). C. Comparison of apoCopC (Tyr79 in green) and Y79W (Trp79 in purple). D. Comparison of Y79W (Trp83 in blue) and Y79WW83F (Phe83 in black), Y79WW83L (Leu83 in yellow). The high hydrophobic region was color in red. The structures in the dished line clearly show the ellipse area in the figure. The structures of mutants come from Phyre. All protein structure displays were created with PyMOL.

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