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Protein Engineering, Vol. 13, No. 3, 193-196, March 2000
© 2000 Oxford University Press

Remarkable thermal stability of doubly intramolecularly cross-linked hen lysozyme

Tadashi Ueda, Kiyonari Masumoto, Ryoji Ishibashi, Takanori So and Taiji Imoto1

Graduate School of Pharmaceutical Sciences, Kyushu University,Fukuoka 812-8582, Japan

In order to examine how a protein can be effectively stabilized, two intramolecular cross-links, Glu35–Trp108 and Lys1–His15, which have few unfavorable interactions in the folded state, were simultaneously introduced into hen lysozyme. Both of the intramolecularly cross-linked lysozymes, 35–108 CL and 1–15 CL, containing cross-links Glu35–Trp108 and Lys1–His15, respectively, showed increases in thermal stability of 13.9 and 5.2°C, respectively, over that of wild type, at pH 2.7. On the other hand, a doubly cross-linked lysozyme showed an increase in thermal stability of 20.8°C over that of wild type, under identical conditions. Since the sum of the differences in denaturation temperature between wild type and each of the cross-linked lysozymes was nearly equal to that between wild type and the doubly cross-linked lysozyme, we suggest that the efficient stabilization of the lysozyme molecule was the direct result of the double intramolecular cross-links.


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