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Literature summary for 3.1.26.4 extracted from

  • Schmitt, T.J.; Clark, J.E.; Knotts, T.A.
    Thermal and mechanical multistate folding of ribonuclease H (2009), J. Chem. Phys., 131, 235101.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Renatured (Commentary)

Renatured (Comment) Organism
study on thermal and mechanical folding and unfolding mechanisms. Mechanical and thermal unfolding proceed through three stable states that are similar. The one difference between the two regimes is in the transition occurring at the most denaturing conditions. For the thermal case, both secondary and tertiary structures melt. For the mechanical case, the secondary structure of the helices remains largely intact, while the bundle itself unfolds. Of the major secondary structure motifs, alpha-helices are more stable than beta-sheets Escherichia coli