Unfolding of tertiary structures of proteins

HIROMITSU WAKANA, HIDEO YOKOMIZO, HIROSHI WAKO, YOSHINORI ISOGAI, KAZUHIKO KOSUGE, NOBUHIKO SAITÔ

研究成果: Article査読

2 被引用数 (Scopus)

抄録

The unfolding pathway of lysozyme was investigated by carrying out the computer simulation. Taking into account the simultaneous change of both the dihedral angles ø and of a residue, we explore the detailed features of the conformational energy profiles. The triangle distance map shows that the lysozyme molecule is divided into three domains, 1–40, 41–101 and 102–129 in amino acid residue numbers (referred to as the domains I, II and III, respectively). The calculated unfolding process indicates that in the early stage of unfolding domain III located at the C‐terminal begins to be detached from the other two, and then domain I can be unfolded. The long‐range interactions between domains I and III stabilize the whole molecule and give the cooperative nature of the folding. The calculated unfolding pathway of lysozyme is consistent with the folding pathway proposed by Anderson & Wetlaufer [J. Biol. Chem. (1976). 251, 3147–3153] who identified the disulfide bondings in the early stage of the glutathione regeneration. A simplified treatment of unfolding for myoglobin is also discussed in the Appendix.

本文言語English
ページ(範囲)657-670
ページ数14
ジャーナルInternational Journal of Peptide and Protein Research
23
6
DOI
出版ステータスPublished - 1984 6

ASJC Scopus subject areas

  • 生化学

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