Using DFT and nudged elastic band calculations on an Aβ fibril-end dimer, the authors find twisted conformations are local minima separated by activation barriers controlled by sidechain steric hindrance.
Eisenberg and Michael R
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Exploration of the potential energy surface for the conformational interconversion of the amyloid $\beta$ peptide at the fibril end
Using DFT and nudged elastic band calculations on an Aβ fibril-end dimer, the authors find twisted conformations are local minima separated by activation barriers controlled by sidechain steric hindrance.