Remarkable thermal stability of doubly intramolecularly cross-linked hen lysozyme

Tadashi Ueda, Kiyonari Masumoto, Ryoji Ishibashi, Takanori So, Taiji Imoto

Research output: Contribution to journalArticlepeer-review

23 Citations (Scopus)


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 crosslinks 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.

Original languageEnglish
Pages (from-to)193-196
Number of pages4
JournalProtein Engineering
Issue number3
Publication statusPublished - 2000
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology


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