Journal of agricultural and food chemistry, 54(23), 8883-8890 (2006-11-09)
Laccase-catalyzed oligomerization of proteins was studied using Trametes hirsuta laccase (ThL) and coactosin as a model system. The reaction mechanism was elucidated using free amino acids and the tripeptide Gly-Leu-Tyr as substrates. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS)
The asymmetric unit (C17H25N3O5.C3H8O.2H2O) consists of two crystallographically independent peptide molecules, A and B, with different conformations, chi 1(2) being trans and gauche- for the Leu residues in molecules A and B, respectively. The backbone conformation of both peptide molecules
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