Are There Folding Pathways in the Functional Stages of Intrinsically Disordered Proteins?
2016 (English)In: Application Of Mathematics In Technical And Natural Sciences (AMITANS'16), 2016, 110008Conference paper (Refereed)
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
AIP Conference Proceedings, ISSN 0094-243X ; 1773
IdentifiersURN: urn:nbn:se:uu:diva-316642DOI: 10.1063/14965012ISI: 000392692400058ISBN: 9780735414310 OAI: oai:DiVA.org:uu-316642DiVA: diva2:1078600
8th International Conference on Promoting the Application of Mathematics in Technical and Natural Sciences (AMiTaNS), JUN 22-27, 2016, Albena, BULGARIA