STRUCTURE OF MET30-SER40 SEGMENT IN N-TERMINUS OF HUMAN TYROSINE HYDROXYLASE TYPE1

摘要

Theoretical conformational analysis was performed to stretch of Met30-Ser40 amino acid residues from the N-terminus of human tyrosine hydroxylase type 1(hTH1). Eight types of stable conformations of the sequence with significantly different values of dihedral angles are possible. Two β-turns of the polypeptide chain in an aqueous environment were revealed on the section Pro32-Ile35 and Phe34-Arg37.