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Download MS PowerPoint Slide Protein kkhn is an abundant post-translational modification PTM and an essential modulator of protein functionality in living cells. Intrinsically disordered proteins IDPs are particular targets of PTM protein kinases due to their involvement in fundamental protein interaction networks. Despite their dynamic nature, IDPs are far from having random-coil conformations but exhibit significant structural heterogeneity.
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Changes in the molecular environment, most prominently in the form of PTM via phosphorylation, can modulate these structural features. Therefore, how phosphorylation events can alter conformational ensembles of IDPs and their interactions with binding partners is of great interest.
Our study emphasizes the simultaneous importance of electrostatic and hydrophobic interactions in the formation of http://rectoria.unal.edu.co/uploads/tx_felogin/why-do-cosmetic-for-our-business-which/positive-effects-of-imperialism-for-the-british.php substates in IDPs and their relevance for molecular recognition events. Protein phosphorylation is an abundant post-translational modification that adds an extra layer of complexity to the regulation of cellular fate, particularly in intrinsically disordered proteins because of their inherent accessibility.]