TY - JOUR T1 - Intrinsically Disordered Proteins Display No Preference for Chaperone Binding In Vivo A1 - Hegyi, Hedi A1 - Tompa, Peter Y1 - 2008/03/07 N2 - Author SummaryIntrinsically disordered/unstructured proteins (IDPs) defy the classical structure–function paradigm because they exist and function without a well-defined 3-D structure. These proteins are extremely sensitive to degradation in the test tube, but show no enhanced degradation rates in the cell. To resolve this apparent contradiction, we tested whether IDPs are protected by interaction with accessory proteins, chaperones, often implicated in guarding other proteins in the cell. Our major finding is that disorder predicted by the IUPred algorithm actually shows negative correlation with chaperone binding in various species. To explain this finding, we argue that IDPs are protected in the cell from proteases by their special amino acid composition, and also by the tight regulation of intracellular proteases. Thus, the primary reason for their chaperone binding is not protection from degradation, but promotion of assembly with partners. JF - PLOS Computational Biology JA - PLOS Computational Biology VL - 4 IS - 3 UR - https://doi.org/10.1371/journal.pcbi.1000017 SP - e1000017 EP - PB - Public Library of Science M3 - doi:10.1371/journal.pcbi.1000017 ER -