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      Function and structure of inherently disordered proteins

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      Current Opinion in Structural Biology
      Elsevier BV

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          Abstract

          The application of bioinformatics methodologies to proteins inherently lacking 3D structure has brought increased attention to these macromolecules. Here topics concerning these proteins are discussed, including their prediction from amino acid sequence, their enrichment in eukaryotes compared to prokaryotes, their more rapid evolution compared to structured proteins, their organization into specific groups, their structural preferences, their half-lives in cells, their contributions to signaling diversity (via high contents of multiple-partner binding sites, post-translational modifications, and alternative splicing), their distinct functional repertoire compared to that of structured proteins, and their involvement in diseases.

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          Author and article information

          Journal
          Current Opinion in Structural Biology
          Current Opinion in Structural Biology
          Elsevier BV
          0959440X
          December 2008
          December 2008
          : 18
          : 6
          : 756-764
          Article
          10.1016/j.sbi.2008.10.002
          18952168
          ec15ea16-a775-451e-ad7e-a906d7455161
          © 2008

          https://www.elsevier.com/tdm/userlicense/1.0/

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