Amyloid formation, like folding of globular proteins, is the outcome of the balance of interaction of peptide main-chain and the packing/solvation of protein side-chains. We have found that two amylodogenic proteins (hIAPP and tau) have different propensities for alpha helical and beta-sheet structure at different temperature range. Using extensive REMD simulations, we found that hIAPP prefers alpha helix at high temperature but beta-sheet structure at room temperature. The result explains the experimental observation of alpha helix intermediates in hIAPP aggregation. However, for tau protein we found that the beta-sheet is stabilized at high temperature and disordered structure is preferred at room temperature. The phenomena imply the cold dissociation of tau protein fibril. Subsequent experiments verified the computational prediction that tau protein fibril may dissociate back to monomers when cooling below room temperature.

Temperature dependent secondary structure transitions in protein aggregation

245th National Meeting (2013)

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