Protein Folding upon Binding Revealed by Molecular Dynamics Simulation
Sign Up to like & getrecommendations! Published in 2017 at "Biophysical Journal"
DOI: 10.1016/j.bpj.2016.11.329
Abstract: Macromolecules frequently associate in living cells and tissues, where specific binding interactions based on dynamic conformation regulate molecular localization and activity. Despite the rapidly expanding experimental characterization of the structural proteome, the combinatorial explosion of… read more here.
Keywords: binding revealed; upon binding; folding upon; protein folding ... See more keywords
Hierarchical folding-upon-binding of an intrinsically disordered protein.
Sign Up to like & getrecommendations! Published in 2025 at "Nature communications"
DOI: 10.1038/s41467-025-66420-5
Abstract: Intrinsically disordered proteins (IDPs) often undergo folding-upon-binding to their partners via short linear motifs, typically 5-15 amino acids in length. However, a significant proportion of IDPs do not adhere to this paradigm but fold upon… read more here.
Keywords: folding upon; intrinsically disordered; disordered protein; folding intermediates ... See more keywords
Folding-upon-binding pathways of an intrinsically disordered protein from a deep Markov state model
Sign Up to like & getrecommendations! Published in 2024 at "Proceedings of the National Academy of Sciences of the United States of America"
DOI: 10.1073/pnas.2313360121
Abstract: Significance The biological functions of intrinsically disordered proteins are often mediated by sequence segments that fold into stable structures upon binding a structured partner protein. The molecular mechanisms by which disordered proteins recognize and bind… read more here.
Keywords: folding upon; intrinsically disordered; markov state; binding pathways ... See more keywords