Analysis of the stabilization of hen lysozyme by helix macrodipole and charged side chain interaction

Hiroyuki Motoshima, Shouhei Mine, Kiyonari Masumoto, Yoshito Abe, Hiroki Iwashita, Yoshio Hashimoto, Yuki Chijiiwa, Tadashi Ueda, Taiji Imoto

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17 Citations (Scopus)


In the N-terminal region of the α-helix of the c-type lysozymes, two Asx residues exist at the 18th and 27th positions. Hen lysozyme has Asp18/Asn27 (18D/27N), and we prepared three mutant lysozymes, Asn18/Asn27 (18N/27N), Asn18/Asp27 (18N/27D), and Asp18/Asp27 (18D/27D). The stability of the wild-type (18D/27N) lysozyme supported the existence of a hydrogen bond between the side chain of Asp18 and the amide group at the N1 position in the α-helix, while the stability of the 18N/27D lysozyme supported the presence of the capping box between the Ser24 (N-cap) and Asp27 residues. Although electrostatic repulsion was observed between Asp18 and Asp27 residues in 18D/27D lysozyme, the dissociation of each residue contributed to stabilizing the B-helix in 18D/27D lysozyme through hydrogen bonding and charge-helix macrodipole interaction. This is the first evidence that two neighboring negative charges at the N-terminus of the helix both increased the stability of the protein.

Original languageEnglish
Pages (from-to)1076-1081
Number of pages6
JournalJournal of biochemistry
Issue number6
Publication statusPublished - Jun 1997
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General Medicine


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