Anchor Residues Govern Binding and Folding of an Intrinsically Disordered Domain.
Sign Up to like & getrecommendations! Published in 2022 at "ACS chemical biology"
DOI: 10.1021/acschembio.2c00619
Abstract: Minimal protein mimics have yielded novel classes of protein-protein interaction inhibitors; however, this success has not been extended to targeting intrinsically disordered proteins, which represent a significant proportion of important therapeutic targets. We sought to… read more here.
Keywords: binding folding; intrinsically disordered; govern binding; anchor residues ... See more keywords
Effects of flexibility and electrostatic interactions on the coupled binding-folding mechanisms of Chz.core and H2A.z-H2B.
Sign Up to like & getrecommendations! Published in 2017 at "Molecular bioSystems"
DOI: 10.1039/c7mb00103g
Abstract: The intrinsically disordered protein (IDP) Chz.core, which is the interaction core of Chz1, shows binding preference to histone variant H2A.z. Although there are several studies on the binding process of Chz.core, the detailed coupled binding-folding… read more here.
Keywords: flexibility; coupled binding; chz core; binding folding ... See more keywords