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Single‐Centre Model for the Active Site of α‐Chymotrypsin
Author(s) -
Vorherr Thomas,
Altmann KarlHeinz,
Mutter Manfred
Publication year - 1986
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.19860690221
Subject(s) - chemistry , chymotrypsin , active site , peptide , stereochemistry , side chain , peptide bond , catalysis , enzyme , polymer , organic chemistry , biochemistry , trypsin
The polymer‐bound heptapeptide H‐Glu‐His‐Pro‐Gly‐Ser‐Gly‐PEGM was designed as a ‘single‐centre model’ for the active site of α‐chymotrypsin. The peptide was synthesized according to the general principles of the liquid‐phase method for peptide synthesis, and its conformational properties were investigated by CD and IR spectroscopy in solution and in the solid state. In harmony with empirical prediction codes, experimental and theoretical conformational considerations, the peptide adopts a β‐turn conformation stabilized by H‐bonds involving the side chains of Glu, His, and Ser. The development of a H‐bonded system similar to the active site of α‐chymotrypsin leads to implications with respect to a possible catalytic activity of the model peptide.