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A Biophysical Analysis of Aspartic Acid Cyclization Coupled to Peptide Bond Cleavage
Author(s) -
Koulopoulos Michael,
Giaccone Zach,
Reitter Julie,
Mills Kenneth
Publication year - 2016
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.30.1_supplement.1083.5
Subject(s) - asparagine , chemistry , protein splicing , peptide bond , residue (chemistry) , peptide , aspartic acid , intein , cleavage (geology) , decarboxylation , rna splicing , histidine , stereochemistry , combinatorial chemistry , catalysis , amino acid , biochemistry , biology , gene , paleontology , fracture (geology) , rna
Protein splicing is the process by which a polypeptide chain, called an intein, catalyzes its excision from two flanking polypeptides, called exteins, concomitant with the exteins ligating together. We are interested in how inteins catalyze the splicing reaction and therefore are studying the third step of the mechanism via a fluorescence‐based assay using a model peptide. Currently, we are analyzing peptide bond cleavage due to cyclization of aspartic acid rather than asparagine, which is promoted at low pH and high temperature. We are currently studying the potential catalytic role of an adjacent histidine residue and carefully determining the influence of pH and temperature on the reaction. Support or Funding Information This material is based upon work supported by the National Science Foundation under grants MCB‐1244089 and MCB‐1517138 and by a Henry Dreyfus Teacher‐Scholar Award (KVM).