Residual Structure Accelerates Binding of Intrinsically Disordered ACTR by Promoting Efficient Folding upon Encounter.
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DOI: 10.1016/j.jmb.2018.12.001
Abstract: Intrinsically disordered proteins (IDPs) often fold into stable structures upon specific binding. The roles of residual structure of unbound IDPs in coupling binding and folding have been under much debate. While many studies emphasize the… read more here.
Keywords: accelerates binding; disordered actr; residual structure; actr helicity ... See more keywords