The folding of knotted proteins remains a mystery both for theoreticians and experimentalists. Despite the development of new models, the driving force for self-tying remains elusive and the principle of minimal frustration cannot be reproduced in silico. In this paper we review different models used to understand protein self-knotting and suggest, how to improve the structure based model to observe efficient folding. Our preliminary results show, that including information about some amino acids properties, or reducing the set of physical contacts may be beneficial for modeling of the knotted protein folding.
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