Significance of Knotted Structures for Function of Proteins and Nucleic Acids - September 17-21, 2014

Significance of Knotted Structures for Function of Proteins and Nucleic Acids

Poster Session I

25 – POS Board 25 Factors Governing Fibril Formation of Proteins: Insights from Lattice and All-atom Simulations Nguyen Truong 1 , Mai Suan Li 2 1 Institute for Computational Science and Technology, Ho Chi Minh City, Vietnam. 2 Institute of Physics PAS, Warsaw, Poland. Fibril formation of proteins and peptides is associated with a large group of major human diseases, including Alzheimer’s disease, prion disorders, amyotrophic lateral sclerosis, type 2 diabetes etc. Therefore, understanding the key factors that govern this process is of paramount importance. The fibrillogenesis of polypeptide chains depends on their intrinsic properties as well as on external conditions. Using simple lattice and all-atom models we show that fibril formation times are strongly correlated with hydrophobicity, charges and population of the so called fibril-prone conformation in monomer state. The higher is the population the faster is the fibril elongation and this dependence may be described by a single exponential function. Our results open a new way to understand the fibrillogenesis of bio-molecules at the monomer level. We have shown that not all of proteins have the propensity to aggregation. We will also discuss the influence of environment with focus on the recently observed dual effect of crowders on aggregation rates of polypeptide chains.

1. Mai Suan Li et al., J. Chem. Phys. 129, 175101 (2008) 2. Mai Suan Li et al, Phys. Rev. Lett. 105, 218101 (2010). 3. H. B. Nam et al., J. Chem. Phys. 132, 165104 (2010)

4. Nguyen Truong Co and M. S. Li, J. Chem. Phys. 137, 095101 (2012) 5. Nguyen Truong Co and Mai Suan Li, J. Chem. Phys. 138, 185101 (2013)

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