- Terminal modifications
- C-terminal amide at Arg29
- Structural modifications
- not recorded
- Stored three-letter notation
- Tyr · Ala · Asp · Ala · Ile · Phe · Thr · Gln · Ser · Tyr · Arg · Lys · Val · Leu · Ala · Gln · Leu · Ser · Ala · Arg · Lys · Leu · Leu · Gln · Asp · Ile · Leu · Ser · Arg
- Sequence notes
- Twenty-nine residues, the tetrasubstituted hGRF(1-29) analog without the drug affinity complex. Against unmodified GRF(1-29), recorded on the sermorelin entry as YADAIFTNSYRKVLGQLSARKLLQDIMSR, the four changes are D-alanine at position 2, glutamine for asparagine at position 8, alanine for glycine at position 15, and leucine for methionine at position 27. Position 2 is the D-enantiomer; oneLetter records it as A because the derivation model does not represent stereochemistry, and the D-configuration is elementally identical to L-alanine, so it is recorded here instead of being lost. The substitution at position 27 removes the only sulfur-containing residue of the parent fragment, which is why this record has no sulfur while sermorelin does.