Protein misfolding and aggregation into amyloid structures is linked with an increasing number of nonneuropathic (either localized or systemic) and neurodegenerative human disorders. In the present review, we compile and describe methods, which have been developed to predict, detect and characterize amyloid and amyloid-like protein deposits. We focus in the state-of-the-art methodologies to study and image amyloid aggregation in-vitro, from qualitative and low-resolution techniques to methods addressed to resolve protein structures at atomic level. We also recapitulate the most relevant literature describing approaches that have been demonstrated to be able to detect and characterize protein aggregation in cells and living organisms, as well as methodologies to report cytotoxicity associated to amyloid formation. Overall, the aim of this review is to illustrate computational and experimental methods to characterize and predict in-vitro and in-vivo amyloid aggregation, providing the readers valuable information to elect the most appropriate techniques at their convenience.