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. 2011 Oct 18;6(10):e26462. doi: 10.1371/journal.pone.0026462

Table 1. N- and C- terminal sequences of the circularly permuted GroEL subunits constructed in this study.

Mutant Corresponding sequence in WT C-terminal sequence N-terminal sequence
CP209 206 Asn-Lys-Pro-Inline graphic Asn-Lys-Pro C N Met-Inline graphic
CP254 251 Ala-Glu-Asp-Inline graphic Ala-Glu-Asp -Val-Ala-Asn C N Met-Ala-Ala-Ala-Gln-Tyr- Inline graphic
CP376 372 Lys-Leu-Gly-Gly-Inline graphic Lys-Leu-Gly -Ala-Asn C N Met-Ala-Gly-Gly-Ala- Inline graphic
CP376-RW 372 Lys-Leu-Gly-Gly-Inline graphic Lys-Leu-Gly-Ala-Asn C N Met-Gly-Ala-Inline graphic

Underlines and <$>\scale 90%\raster="rg1"<$>wavy underlines are added to highlight corresponding sequence elements between each CP mutant and wild type (WT). Sequences in italics denote amino acids that are not from the native sequence of GroEL, added as a consequence of the circular permutation protocol. In addition, we found that in CP376, the N-terminal amino acid sequence had been altered, and apparently insertion of an extra alanine residue had occurred (double underlined). We decided to name this mutant CP376 based on the fact that the native GroEL amino acid sequence continues uninterrupted after Val376. GroEL CP376-RW contains an additional Arg to Trp point mutation at the position corresponding to Arg231 in the wild type sequence.