Similarity of force-induced unfolding of apomyoglobin to its chemical-induced unfolding: An atomistic molecular dynamics simulation approach

Ho Sup Choi, June Huh, Won Ho Jo

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

We have compared force-induced unfolding with traditional unfolding methods using apomyoglobin as a model protein. Using molecular dynamics simulation, we have investigated the structural stability as a function of the degree of mechanical perturbation. Both anisotropic perturbation by stretching two terminal atoms and isotropic perturbation by increasing the radius of gyration of the protein show the same key event of force-induced unfolding. Our primary results show that the native structure of apomyoglobin becomes destabilized against the mechanical perturbation as soon as the interhelical packing between the G and H helices is broken, suggesting that our simulation results share a common feature with the experimental observation that the interhelical contact is more important for the folding of apomyoglobin than the stability of individual helices. This finding is further confirmed by simulating both helix destabilizing and interhelical packing destabilizing mutants.

Original languageEnglish
Pages (from-to)1492-1502
Number of pages11
JournalBiophysical Journal
Volume85
Issue number3
DOIs
Publication statusPublished - 2003 Sep 1
Externally publishedYes

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ASJC Scopus subject areas

  • Biophysics

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