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Syntehsis and structural stability of helichrome as an artificial hemeproteins
Author(s) -
Sasaki Tomikazu,
Kaiser Emil Thomas
Publication year - 1990
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360290112
Subject(s) - chemistry , guanidine , globular protein , thioanisole , denaturation (fissile materials) , protein folding , folding (dsp implementation) , crystallography , computational chemistry , biochemistry , electrical engineering , nuclear chemistry , engineering , catalysis
A detailed procedure is described for the syntehsis of helichrome, which is the first successful example of polypeptide‐based artificial hemeprotein. The segment synthesis‐condensation approach used for the assembly of small proteins has proven to be extremely useful for protein mimetics as well. The final deprotection was performed using the TNSOTf‐thioanisole method instead of the less‐convenient hydrogen fluoride method. The unfolding transition of the α‐helical conformation of helichrome induced by guanidine hydrochloride was studied to understand the stability and dynamics of the folded structure. The resulting parameters ( C 0.5 = 5.2 M and Δ G H2O = −4.4 kcal mol −1 ) characterizing helichrome denaturation were comparable to that of native globular proteins.