Biology – Quantitative Biology – Biomolecules
Scientific paper
2008-10-02
PNAS 105 (2008) 19714
Biology
Quantitative Biology
Biomolecules
23 pages, 12 figures
Scientific paper
10.1073/pnas.0805468105
Molecular dynamics studies within a coarse-grained structure based model were used on two similar proteins belonging to the transcarbamylase family to probe the effects in the native structure of a knot. The first protein, N-acetylornithine transcarbamylase, contains no knot whereas human ormithine transcarbamylase contains a trefoil knot located deep within the sequence. In addition, we also analyzed a modified transferase with the knot removed by the appropriate change of a knot-making crossing of the protein chain. The studies of thermally- and mechanically-induced unfolding processes suggest a larger intrinsic stability of the protein with the knot.
Cieplak Marek
Sułkowska Joanna I.
Sułkowski Piotr
Szymczak Piotr
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