Unfolding of tertiary structures of proteins

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

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2 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)657-670
Number of pages14
JournalInternational Journal of Peptide and Protein Research
Volume23
Issue number6
DOIs
Publication statusPublished - 1984 Jun

Keywords

  • conformational energy calculation
  • folding pathway
  • lysozyme
  • myoglobin
  • triangle distance map

ASJC Scopus subject areas

  • Biochemistry

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    WAKANA, HIROMITSU., YOKOMIZO, HIDEO., WAKO, HIROSHI., ISOGAI, YOSHINORI., KOSUGE, KAZUHIKO., & SAITÔ, NOBUHIKO. (1984). Unfolding of tertiary structures of proteins. International Journal of Peptide and Protein Research, 23(6), 657-670. https://doi.org/10.1111/j.1399-3011.1984.tb03139.x