TY - JOUR T1 - Influence of Sequence Changes and Environment on Intrinsically Disordered Proteins A1 - Mohan, Amrita A1 - Uversky, Vladimir N. A1 - Radivojac, Predrag Y1 - 2009/09/04 N2 - Author Summary Intrinsically disordered proteins, proteins that exist as conformational ensembles without time-invariant residue positions, have emerged as an important and common class of proteins in all kingdoms of life. Disordered proteins are characterized by distinct amino acid preferences, distinct mechanisms of binding, distinct substitution patterns and rates of evolution, and functional roles predominantly related to signaling and regulation. In recent years, disordered proteins have also been linked to human disease, both through conformational diseases or via host-pathogen interactions. However, despite increased importance, most studies of disordered proteins do not consider the environmental context in which the protein is found or the level of sequence change that would strongly influence the property of being disordered. To address this, we studied and quantified the variability of intrinsically disordered protein regions under different external conditions, such as temperature or pH, and compared them to the variability introduced by small sequence changes. We found that both have a strong impact on the existence of disordered regions, thus potentially regulating protein function by environmental factors or facilitating evolutionary change. JF - PLOS Computational Biology JA - PLOS Computational Biology VL - 5 IS - 9 UR - https://doi.org/10.1371/journal.pcbi.1000497 SP - e1000497 EP - PB - Public Library of Science M3 - doi:10.1371/journal.pcbi.1000497 ER -