Literature DB >> 31783325

Dynamic multivalent interactions of intrinsically disordered proteins.

Jingwei Weng1, Wenning Wang2.   

Abstract

Protein-protein interactions involving intrinsically disordered proteins (IDPs) usually display dynamic and multivalent features. Recent experimental data revealed myriad functional roles of the dynamic multivalent interaction (DMI) of IDPs. However, characterization of DMI remains a challenge due to its complex and promiscuous nature. Recent studies start showing that understanding the mechanistic role of DMI relies on combined use of various techniques and construction of microscopic models in elucidating the binding thermodynamics and kinetics.
Copyright © 2019 Elsevier Ltd. All rights reserved.

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Year:  2019        PMID： 31783325     DOI： 10.1016/j.sbi.2019.11.001

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN： 0959-440X            Impact factor:   6.809


  14 in total

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