Figure 1
Figure 1. CD spectra of MCFD2 proteins. (A) Sequences of the 2 EF-hand domains of MCFD2. Sequences are aligned to match the locations of 6 Ca2+ coordination residues in the Ca2+-binding loops, which are indicated with asterisks. Residues that are mutated in F5F8D patients are shown in boldface, and mutations are indicated by arrows. Amino acid residues in the 4 α-helical regions are shown in italics and are boxed in light gray shade. (B) CD spectra of the wild-type MCFD2, and the D89A, the D122V, and the I136T mutants. The x-axis represents the wavelengths scanned. The y-axis shows molar ellipticity (Mol. Ellip.) values expressed as degrees cm2/dmol.

CD spectra of MCFD2 proteins. (A) Sequences of the 2 EF-hand domains of MCFD2. Sequences are aligned to match the locations of 6 Ca2+ coordination residues in the Ca2+-binding loops, which are indicated with asterisks. Residues that are mutated in F5F8D patients are shown in boldface, and mutations are indicated by arrows. Amino acid residues in the 4 α-helical regions are shown in italics and are boxed in light gray shade. (B) CD spectra of the wild-type MCFD2, and the D89A, the D122V, and the I136T mutants. The x-axis represents the wavelengths scanned. The y-axis shows molar ellipticity (Mol. Ellip.) values expressed as degrees cm2/dmol.

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