Dynamic protein interactions probed by NMR spectroscopy

Dynamic protein–protein interactions are essential for diverse cellular processes but often evade structural characterization due to their transient, heterogeneous, and disordered nature. This review focuses on how nuclear magnetic resonance (NMR) spectroscopy can provide detailed, residue‐level ins...

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Bibliographic Details
Published inBulletin of the Korean Chemical Society Vol. 46; no. 7; pp. 680 - 690
Main Authors Lee, Jaeseok, Lee, Jung Ho
Format Journal Article
LanguageEnglish
Published Weinheim Wiley‐VCH Verlag GmbH & Co. KGaA 01.07.2025
Subjects
dynamic protein interactions
fuzzy interactions
intrinsically disordered proteins
NMR spectroscopy
protein–protein interactions
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ISSN1229-5949
1229-5949
DOI10.1002/bkcs.70036

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Summary:Dynamic protein–protein interactions are essential for diverse cellular processes but often evade structural characterization due to their transient, heterogeneous, and disordered nature. This review focuses on how nuclear magnetic resonance (NMR) spectroscopy can provide detailed, residue‐level insights into these complex interactions. By categorizing dynamic interactions into three distinct yet interconnected classes—(1) interactions with multiple binding interfaces, (2) interactions retaining disorder, and (3) interactions that stabilize or induce disorder—we provide a framework for interpreting diverse interaction modes. Through representative case studies, we highlight the value of NMR in decoding dynamic interactions, where disorder and flexibility persist even in high‐affinity complexes.
ISSN:1229-5949
1229-5949
DOI:10.1002/bkcs.70036