Based on physico-chemical principles of secondary structure formation extended by the assumption that the core regions of an aggregate are fully buried.
Prediction of 'aggregation-prone' in protein sequences, based on an aggregation propensity scale for natural amino acids derived from in vivo experiments.
Structure based prediction of fribrillation propoensities, using crystal strucutrue of the fibril forming peptide NNQQNY from the sup 35 prion protein of Saccharomyces cerevisiae.
Amyloidogenic patterns, average packing density, beta-strand contiguity, pafig, Net-CSSP, STITCHER Amyloidogenic patterns, average packing density, beta-strand contiguity, pafig, Net-CSSP, STITCHER Predicts the most aggregation-prone portions and the corresponding β-strand inter-molecular pairing for multiple input sequences.
Amyloidogenicity propensity predictor based on a machine learning approach through recursive feature selection and feed-forward neural networks, taking advantage of newly published sequences with experimental, in vitro, evidence of amyloid formation.