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  • The formation of the fluorescent protein FP611 chromophore cross-link from the alpha-carboxyl carbon of residue n, a methionine, to the alpha-amino nitrogen of residue n+2, a glycine, and a dehydration to form a double bond to the alpha-amino nitrogen of residue n+1. This cross-linking is coupled with a dehydrogenation of residue n+1 to form a double bond between the alpha and beta carbons. This modification is found in the GFP-like fluorescent chromoprotein from the sea anemone Entacmaea quadricolor. [PDB:1UIS, PDB:1XQM, PMID:10852900, PMID:12185250, PMID:12909624, PMID:15542608, RESID:AA0379]
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