Structure determination of amyloid fibrils

Dr. Itzam De Gortari, Dr M Segall, Prof. M Payne

The term amyloid fibril refers to a protein that has self-assembled into an insoluble pleated sheet structure. Here we seek to apply quantum mechanical ab initio techniques to systems of an interesting scale in molecular biology for the understanding of amyloidal diseases. A considerable amount of experimental data motivates our work to investigate theoretical mechanisms that break protein bonds in fibrils. Thus, we propose a systematic study by means of calculated NMR Chemical Shifts of polypeptides in different conformations. Particular attention is given to conformations associated with the formation of beta sheets, since these are the main links in the amyloid fibrils.