How knots influence properties of proteins

Preprint

2 October 2008

preprint
Published by arXiv in arXiv

https://doi.org/10.48550/arXiv.0810.0415

Abstract

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.

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Version 1, 2008-10-02, ArXiv
Published version: Proceedings of the National Academy of Sciences, 105 (50), 19714.

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