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Figure 1

Figure 1. From: INVESTIGATIONS INTO TROPOMYOSIN FUNCTION USING MOUSE MODELS.

Multiple sequence alignments of the mouse striated muscle Tm isoforms. The complete protein sequence (amino acids 1-284) for the striated muscle α-Tm, β-Tm, and γ-Tm isoforms were aligned. Comparisons of the amino acid biophysical properties are color coded and indicated by dots below the amino acid sequence, as designated in the legend. Chimera 1 sequences that were exchanged from α-Tm to β-Tm are underlined (amino acids 258-284). Chimera 3 sequences that were exchanged from α-Tm to β-Tm are double underlined (amino acids 175-190). Chimera 2 sequences exchanged both regions from α-Tm to β-Tm (amino acids 175-190 and 258-284). The mouse skeletal muscle α-Tm, β-Tm and γ-Tm nucleotide sequences are accession numbers X64831, M81086, and AF317223, respectively. The amino acid sequence analysis was conducted according to methods described in Larkin et al. ().

Ganapathy Jagatheesan, et al. J Mol Cell Cardiol. ;48(5):893-898.

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