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Literature summary for 3.2.1.17 extracted from

  • Peng, Q.; Li, H.
    Atomic force microscopy reveals parallel mechanical unfolding pathways of T4 lysozyme: evidence for a kinetic partitioning mechanism (2008), Proc. Natl. Acad. Sci. USA, 105, 1885-1890.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Tequatrovirus T4 P00720
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Renatured (Commentary)

Renatured (Comment) Organism
on stretching from its N and C termini using single-molecule atomic force microscopy, T4 lysozyme unfolds by multiple distinct unfolding pathways: the majority of T4 lysozymes unfold in an all-or-none fashion by overcoming a dominant unfolding kinetic barrier; and a small fraction of T4 lysozymes unfold in three-state fashion involving unfolding intermediate states. Results give direct evidence for the kinetic partitioning of the mechanical unfolding pathways of T4 lysozyme, and the complex unfolding behaviors reflect the stochastic nature of kinetic barrier rupture in mechanical unfolding processes Tequatrovirus T4