Unfolding Pathways of Goat α-Lactalbumin as Revealed in Multiple Alignment of Molecular Dynamics Trajectories

Tomotaka Oroguchi, Mitsunori Ikeguchi, Motonori Ota, Kunihiro Kuwajima, Akinori Kidera

研究成果: Article

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Molecular dynamics simulations of protein unfolding were performed at an elevated temperature for the authentic and recombinant forms of goat α-lactalbumin. Despite very similar three-dimensional structures, the two forms have significantly different unfolding rates due to an extra N-terminal methionine in the recombinant protein. To identify subtle differences between the two forms in the highly stochastic kinetics of unfolding, we classified the unfolding trajectories using the multiple alignment method based on the analogy between the biological sequences and the molecular dynamics trajectories. A dendrogram derived from the multiple trajectory alignment revealed a clear difference in the unfolding pathways of the authentic and recombinant proteins, i.e. the former reached the transition state in an all-or-none manner while the latter unfolded less cooperatively. It was also found in the classification that the two forms of the protein shared a common transition state structure, which was in excellent agreement with the transition state structure observed experimentally in the Φ-value analysis.

元の言語English
ページ(範囲)1354-1364
ページ数11
ジャーナルJournal of Molecular Biology
371
発行部数5
DOI
出版物ステータスPublished - 2007 8 31
外部発表Yes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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