Unified understanding of folding and binding mechanisms of globular and intrinsically disordered proteins
Sign Up to like & getrecommendations! Published in 2017 at "Biophysical Reviews"
DOI: 10.1007/s12551-017-0346-7
Abstract: Extensive experimental and theoretical studies have advanced our understanding of the mechanisms of folding and binding of globular proteins, and coupled folding and binding of intrinsically disordered proteins (IDPs). The forces responsible for conformational changes… read more here.
Keywords: binding globular; folding binding; rate; globular proteins ... See more keywords
Protein folding, binding, and droplet formation in cell-like conditions.
Sign Up to like & getrecommendations! Published in 2017 at "Current opinion in structural biology"
DOI: 10.1016/j.sbi.2016.10.006
Abstract: The many bystander macromolecules in the crowded cellular environments present both steric repulsion and weak attraction to proteins undergoing folding or binding and hence impact the thermodynamic and kinetic properties of these processes. The weak… read more here.
Keywords: droplet formation; folding binding; formation cell; droplet ... See more keywords
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
Sign Up to like & getrecommendations! Published in 2017 at "PLoS Computational Biology"
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
Folding and Binding Mechanisms of the SH2 Domain from Crkl
Sign Up to like & getrecommendations! Published in 2022 at "Biomolecules"
DOI: 10.3390/biom12081014
Abstract: SH2 domains are structural modules specialized in the recognition and binding of target sequences containing a phosphorylated tyrosine residue. They are mostly incorporated in the 3D structure of scaffolding proteins that represent fundamental regulators of… read more here.
Keywords: sh2 domain; mechanisms sh2; domain crkl; binding mechanisms ... See more keywords