How knots influence properties of proteins

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dc.creatorSułkowska, Joanna I.
dc.creatorSułkowski, Piotr
dc.creatorSzymczak, P.
dc.creatorCieplak, Marek
dc.date2008-10-02
dc.date.accessioned2026-07-07T12:41:49Z
dc.date.available2026-07-07T12:41:49Z
dc.descriptionMolecular 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.
dc.description23 pages, 12 figures
dc.identifierhttps://arxiv.org/abs/0810.0415
dc.identifierhttp://arxiv.org/abs/0810.0415
dc.identifierPNAS 105 (2008) 19714
dc.identifierdoi:10.1073/pnas.0805468105
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/219868
dc.subjectBiomolecules
dc.titleHow knots influence properties of proteins
dc.typetext

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