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- W1515706086 endingPage "550" @default.
- W1515706086 startingPage "539" @default.
- W1515706086 abstract "The past decade has witnessed great advances in our understanding of protein structure-function relationships in terms of the ubiquitous existence of intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs). The structural disorder of IDPs/IDRs enables them to play essential functions that are complementary to those of ordered proteins. In addition, IDPs/IDRs are persistent in evolution. Therefore, they are expected to possess some advantages over ordered proteins. In this review, we summarize and survey nine possible advantages of IDPs/IDRs: economizing genome/protein resources, overcoming steric restrictions in binding, achieving high specificity with low affinity, increasing binding rate, facilitating posttranslational modifications, enabling flexible linkers, preventing aggregation, providing resistance to non-native conditions, and allowing compatibility with more available sequences. Some potential advantages of IDPs/IDRs are not well understood and require both experimental and theoretical approaches to decipher. The connection with protein design is also briefly discussed." @default.
- W1515706086 created "2016-06-24" @default.
- W1515706086 creator A5043308504 @default.
- W1515706086 creator A5080579774 @default.
- W1515706086 date "2014-03-17" @default.
- W1515706086 modified "2023-10-16" @default.
- W1515706086 title "Advantages of proteins being disordered" @default.
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