Free Energy Profile and Kinetics of Coupled Folding and Binding of the Intrinsically Disordered Protein p53 with MDM2
Sign Up to like & getrecommendations! Published in 2020 at "Journal of chemical information and modeling"
DOI: 10.1021/acs.jcim.9b00920
Abstract: Intrinsically disordered proteins (IDPs) exert their functions by binding to partner proteins via a complex process that includes coupled folding and binding. Motivated by that inhibiting the binding of the IDP p53 to its partner… read more here.
Keywords: folding binding; coupled folding; process; p53 ... See more keywords
Dissecting mechanism of coupled folding and binding of an intrinsically disordered protein by chemical synthesis of conformationally constrained analogues.
Sign Up to like & getrecommendations! Published in 2017 at "Chemical communications"
DOI: 10.1039/c7cc02276j
Abstract: Non-canonical α-methyl amino acids were incorporated at various sites in the sequence of intrinsically disordered activation domain from the p160 transcriptional co-activator (ACTR) to facilitate the formation of α-helical structures. Kinetic and thermodynamic data confirm… read more here.
Keywords: folding binding; mechanism; coupled folding; mechanism coupled ... See more keywords
Role of non-native electrostatic interactions in the coupled folding and binding of PUMA with Mcl-1
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DOI: 10.1371/journal.pcbi.1005468
Abstract: PUMA, which belongs to the BH3-only protein family, is an intrinsically disordered protein (IDP). It binds to its cellular partner Mcl-1 through its BH3 motif, which folds upon binding into an α helix. We have… read more here.
Keywords: role non; folding binding; coupled folding; native electrostatic ... See more keywords