Relative solvent accessible surface area predicts protein conformational changes upon binding

HIGHLIGHTS

  • who: Joseph A. Marsh from the of Molecular Biology, Hills Road, Cambridge , QH, UK have published the Article: Relative Solvent Accessible Surface Area Predicts Protein Conformational Changes upon Binding, in the Journal: (JOURNAL)
  • what: The authors observe considerable enrichment of intrinsically disordered sequences in proteins predicted to undergo large Finally the authors demonstrate that the of monomeric proteins can be used as a simple proxy for flexibility. The authors start with an approach that may be considered the opposite of docking: given the known structure of a protein complex, the authors seek to predict the . . .

     

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