Xue, BinDunker, A. KeithUversky, Vladimir N.2018-07-272018-07-272010-09-29Xue, B., Dunker, A. K., & Uversky, V. N. (2010). Retro-MoRFs: Identifying Protein Binding Sites by Normal and Reverse Alignment and Intrinsic Disorder Prediction. International Journal of Molecular Sciences, 11(10), 3725–3747. https://doi.org/10.3390/ijms111037251422-0067https://hdl.handle.net/1805/16867Many cell functions in all living organisms rely on protein-based molecular recognition involving disorder-to-order transitions upon binding by molecular recognition features (MoRFs). A well accepted computational tool for identifying likely protein-protein interactions is sequence alignment. In this paper, we propose the combination of sequence alignment and disorder prediction as a tool to improve the confidence of identifying MoRF-based protein-protein interactions. The method of reverse sequence alignment is also rationalized here as a novel approach for finding additional interaction regions, leading to the concept of a retro-MoRF, which has the reversed sequence of an identified MoRF. The set of retro-MoRF binding partners likely overlap the partner-sets of the originally identified MoRFs. The high abundance of MoRF-containing intrinsically disordered proteins in nature suggests the possibility that the number of retro-MoRFs could likewise be very high. This hypothesis provides new grounds for exploring the mysteries of protein-protein interaction networks at the genome level.en-USAttribution 3.0 United Statesreverseretroinvertalignmentintrinsic disorderPONDR-RIBSArticle