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Updated: May 21, 2025

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
Published on: November 1, 2024
Toward understanding biomolecular materials comprising intrinsically disordered proteins via simulation and
Bin Wang1, Tianren Zhang1,2, Sirui Shen1
1Department of Materials Science and Engineering, University of Delaware Newark DE USA kiick@udel.edu.
None:
Intrinsically disordered proteins (IDPs) yield solutions with tunable phase transition behavior and have been widely applied in designing stimuli-responsive materials. Understanding interactions between amino acid residues of the IDP sequence is critical to designing new IDP-based materials with selective phase behavior, assembly, and mechanical properties. The lack of defined structure for this class of proteins complicates accurate prediction of their molecular-scale behavior. In this review, recent progress is presented in the development and application of simulation methods to describe the behavior of IDPs. Results for elastin-like polypeptides (ELPs) and resilin-like polypeptides (RLPs) are highlighted, focusing on studies that compare simulation results with experimental findings.
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