Atomically detailed description of the unfolding of α-lactalbumin by the combined use of experiments and simulations

Tomotaka Oroguchi, Mitsunori Ikeguchi, Kimiko Saeki, Kiyoto Kamagata, Yoriko Sawano, Masaru Tanokura, Akinori Kidera, Kunihiro Kuwajima

研究成果: Article査読

7 被引用数 (Scopus)

抄録

The recombinant form of goat α-lactalbumin has a significantly faster unfolding rate compared to the authentic form, although the two molecules differ only in an extra methionine at the N terminus of the recombinant. The mechanism of the destabilization caused by this residue was investigated through the combined use of kinetic experiments and molecular dynamics simulations. Unfolding simulations for the authentic and recombinant forms at 398 K (ten trajectories of 5 ns for each form, 100 ns total) precisely reproduced the experimentally observed differences in unfolding behavior. In addition, experiments reproduced the destabilization of a mutant protein, T38A, faithfully as predicted by the simulations. This bidirectional verification between experiments and simulations enabled the atomically detailed description of the role of the extra methionine residue in the unfolding process.

本文言語English
ページ(範囲)164-172
ページ数9
ジャーナルJournal of Molecular Biology
354
1
DOI
出版ステータスPublished - 2005 11 18
外部発表はい

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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