PT - JOURNAL ARTICLE AU - MichaƂ S Barski TI - BASILIScan: a tool for high-throughput analysis of intrinsic disorder patterns in homologous proteins AID - 10.1101/378018 DP - 2018 Jan 01 TA - bioRxiv PG - 378018 4099 - http://biorxiv.org/content/early/2018/07/26/378018.short 4100 - http://biorxiv.org/content/early/2018/07/26/378018.full AB - Background Intrinsic structural disorder is a common property of many proteins, especially in eukaryotic and virus proteomes. The tendency of some proteins or protein regions to exist in a disordered state usually precludes their structural characterisation and renders them especially difficult for experimental handling after recombinant expression.Results A new intuitive, publicly-available computational resource, called BASILIScan, is presented here. It provides a BLAST-based search for close homologues of the protein of interest, integrated with a simultaneous prediction of intrinsic disorder together with a robust data viewer and interpreter. This allows for a quick, high-throughput screening, scoring and selection of closely-related yet highly structured homologues of the protein of interest. Comparative parallel analysis of the conservation of extended regions of disorder in multiple sequences is also offered. The use of BASILIScan and its capacity for yielding biologically applicable predictions is demonstrated. Using a high-throughput BASILIScan screen it is also shown that a large proportion of the human proteome displays homologous sequences of superior intrinsic structural order in many related species.Conclusion Through the swift identification of intrinsically stable homologues and poorly conserved disordered regions by the BASILIScan software, the chances of successful recombinant expression and compatibility with downstream applications such as crystallisation can be greatly increased.