Article

Optimal Anchoring of a Urea-based Foldamer Inhibitor of ASF1 Histone Chaperone Through Backbone Plasticity

2020-07-09

Abstract excerpt

Sequence-specific oligomers with predictable folding patterns, i.e. foldamers provide new opportunities to mimic α-helical peptides and design inhibitors of protein-protein interactions. One major hurdle of this strategy is to retain the correct orientation of key side chains involved in protein surface recognition. Here, we show that the structural plasticity of a foldamer backbone may significantly contrib...

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Literature Corpus work: fe9de305-7ec6-5370-a598-34b73b3ce660
DOI: 10.26434/chemrxiv.12624722.v1

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Optimal Anchoring of a Urea-based Foldamer Inhibitor of ASF1 Histone Chaperone Through Backbone PlasticityDOI 10.26434/chemrxiv.12624722.v1Read

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