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Are There Folding Pathways in the Functional Stages of Intrinsically Disordered Proteins?
Inst Informat & Commun Technol BAS, Sofia, Bulgaria..
Beijing Inst Technol, Sch Phys, Beijing, Peoples R China..
Sofia Univ St Kliment Ohridski, Fac Phys, Sofia, Bulgaria..
Sofia Univ St Kliment Ohridski, Fac Phys, Sofia, Bulgaria..
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2016 (English)In: Application Of Mathematics In Technical And Natural Sciences (AMITANS'16), 2016, 110008Conference paper, Published paper (Refereed)
Abstract [en]

We proceed from the description of protein folding by means of molecular dynamics (MD) simulations with all-atom force fields, with folding pathways interpreted in terms of soliton structures, to identify possible systematic dynamical patterns of self-organisation that govern protein folding process. We perform in silico investigations of the conformational transformations of three different proteins MYC protein (an alpha-helical protein), amylin and indolicidin (IDPs with different length and binding dynamics). We discuss the emergence of soliton-mediated secondary motifs, in the case of IDPs in the context of their functional activity. We hypothesize that soliton-like quasi-ordered conformations appear as an important intermediate stage in this process.

Place, publisher, year, edition, pages
2016. 110008
Series
AIP Conference Proceedings, ISSN 0094-243X ; 1773
National Category
Physical Sciences
Identifiers
URN: urn:nbn:se:uu:diva-316642DOI: 10.1063/14965012ISI: 000392692400058ISBN: 9780735414310 (print)OAI: oai:DiVA.org:uu-316642DiVA: diva2:1078600
Conference
8th International Conference on Promoting the Application of Mathematics in Technical and Natural Sciences (AMiTaNS), JUN 22-27, 2016, Albena, BULGARIA
Available from: 2017-03-06 Created: 2017-03-06 Last updated: 2017-03-06Bibliographically approved

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Niemi, Antti J.

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