Secondary structural changes of chymotrypsinogen A, alpha-chymotrypsin, and the isolated polypeptides Cys¹-Leu¹³, Ile¹⁶-Tyr¹⁴⁶, and Ala¹⁴⁹-Asn²⁴⁵ in sodium dodecyl sulfate, urea and guanidine hydrochloride

Abstract

Secondary structural changes of chymotrypsinogen A,α-chymotrypsin, and their isolated polypeptides Cys¹-Leu¹³, Ile¹⁶-Tyr¹⁴⁶, and Ala¹⁴⁹-Asn²⁴⁵were examined in aqueous solutions of sodium dodecyl sulfate (SDS), urea, and guanidine hydrochloride (residue numbers from chymotrypsinogen). After the fragmentation by the cleavage of disulfide bridges inα-chymotrypsin, the helical structure was formed in the isolated polypeptide 16–146 where the helical segments do not exist in the protein state. The polypeptide 149–245, where the helical segments of the parent protein are originally located, contained no helices. The polypeptide 1–13 was almost disordered. The three polypeptides, chymotrypsinogen,α-chymotrypsin and the polypeptide 16–146, clearly showed differences in the stabilities of helical structures in solutions of urea and guanidine hydrochloride. The addition of SDS accelerated the formation of helical structures in each polypeptide except for 1–13.