The structure of the transmembrane domain of the Amyloid Precursor Protein has been studied as a function of sequence and lipid composition using a multiscale simulation approach that combines atomistic and coarse-grained models. The simulation results demonstrate that the C99 homodimer structure consists of a conformational ensemble with multiple structural states stabilized by distinctive interpeptide interactions. The relative probability of each conformational state can be modulated through the membrane environment.

Impact of membrane composition on the structure, stability, and processing of the transmembrane domain of the amyloid precursor p

249th National Meeting (2015)

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