• Small polymorphic oligomers (cylindrin) are cytotoxic and related to neurodegenerative diseases.
• The atomic structure of cylindrin formed by six identical 11-residue β-strands that adopt a β-barrel conformation, exhibiting strong intra- and inter-strand H-bonds.
• Extensive molecular dynamics simulations, comparing five different force fields (CHARMM36, ff99SB, ff14SB, OPLS- AA, OLPS-AA/M).
• Salt-bridges does not contribute to the stability of cylindrin, as observed for the five force fields.
• All-alanine mutants showed that H-bonds are not enough to keep the protein structure stable, where hydrophobic interactions in the hydrophobic core seem to be the determinant for the formation of cylindrin.
• Nevertheless significant differences were observed between the force fields for the latter, so further examination is required.

Identification of noncovalent interactions driving the folding of cylindrin-like structures using theoretical calculations

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