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Journal of Protein Chemistry

, Volume 12, Issue 2, pp 121–131 | Cite as

Refolding of cytochromeb562 and its structural stabilization by introducing a disulfide bond

  • Yukio Kobayashi
  • Hiroyuki Sasabe
  • Nobuhiko Saitô
Article

Abstract

The packing mechanism of the secondary structures (4-α-helices and 310-helix) of cytochromeb562 is simulated by the “island model,” where the formation of protein structure is accomplished by the growth-type mechanism with the driving force of packing of the long-range and specific hydrophobic interactions. Packing proceeds through the formation of the structure at the nonhelical part, where a lot of hydrophobic pairs are distributed. Consequently, conformation, nearly similar to the native one, is successfully obtained. With the help of this result, the theoretical prediction of the possibility of forming this disulfide mutant (N22C/G82C) ofb562 can be performed prior to the experiments by our geometrical criterion (“lampshade”). This criterion is expected to be a significant principle for introducing possible disulfide bonds into a protein to be engineered.

Key words

Cytochromeb562 disulfide mutant island model site-directed mutagenesis 4-α-helical packing 

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Copyright information

© Plenum Publishing Corporation 1993

Authors and Affiliations

  • Yukio Kobayashi
    • 1
  • Hiroyuki Sasabe
    • 1
  • Nobuhiko Saitô
    • 2
  1. 1.Frontier Research ProgramThe Institute of Physical and Chemical Research (RIKEN)Wako, SaitamaJapan
  2. 2.Department of Applied PhysicsWaseda UniversityTokyoJapan

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