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Table 1 Peptides used in this study

From: Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD

Name Sequence Charge Source
UniProt Position
S2 TRYWNPKMKPFIFGA +3 P0A7V0 20–34
S2-minus1 GHQTRYWNPKMKPFI +3 to +4   17–31
S2-minus2 VHFGHQTRYWNPKMK +3 to +5   14–28
S2-minus3 KAGVHFGHQTRYWNP +2 to +4   11–25
S2-plus1 WNPKMKPFIFGARNK +4   23–37
S2-plus2 KMKPFIFGARNKVHI +4 to +5   26–40
S2-long2 QTRYWNPKMKPFIFGAR +4   19–35
S2-long4 HQTRYWNPKMKPFIFGARN +4 to +5   18–36
S2-long6 GHQTRYWNPKMKPFIFGARNK +5 to +6   17–37
S2-long8 FGHQTRYWNPKMKPFIFGARNKV +5 to +6   16–38
S2-short2 RYWNPKMKPFIFG +3   21–33
S2-short4 YWNPKMKPFIF +2   22–32
S2-short6 WNPKMKPFI +2   23–31
S2-short8 WNPKMKP +2   23–29
S3 RLGIVKPWNSTWFAN +2 P0A7V3 11–25
T1 VGSNSYPHKYNNYEG 0 to +1 P00651 59–73
SlpA linker SGLVPRGS +1 - -
  1. For peptides derived from the S2 protein, parts overlapping the original S2 peptide are underlined. The expected charges at neutral pH are listed. These were calculated using −1 for Glu and Asp, +1 for Lys and Arg, and 0 or +1 for His (for peptides with His residues, the charge is given as a range). In addition to the peptides listed here, we also used the following five mutants of the S2 peptide: P25A, P29E, P25A/P29E, P25N/P29N, and W23A