Mechanism of Coupled Folding-upon-Binding of an Intrinsically Disordered Protein

Intrinsically disordered proteins (IDPs), which in isolation do not adopt a well-defined tertiary structure but instead populate a structurally heterogeneous ensemble of interconverting states, play important roles in many biological pathways. IDPs often fold into ordered states upon binding to thei...

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Veröffentlicht in:	Journal of the American Chemical Society 2020-06, Vol.142 (25), p.11092-11101
Hauptverfasser:	Robustelli, Paul, Piana, Stefano, Shaw, David E
Format:	Artikel
Sprache:	eng
Schlagworte:	Intrinsically Disordered Proteins - chemistry Intrinsically Disordered Proteins - metabolism Measles virus - chemistry Molecular Dynamics Simulation Nucleocapsid Proteins - chemistry Nucleocapsid Proteins - metabolism Peptide Fragments - chemistry Peptide Fragments - metabolism Phosphoproteins - chemistry Phosphoproteins - metabolism Protein Binding Protein Conformation, alpha-Helical Protein Domains Protein Folding
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