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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| Published in | Bulletin of the Korean Chemical Society Vol. 46; no. 7; pp. 680 - 690 |
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| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
Weinheim
Wiley‐VCH Verlag GmbH & Co. KGaA
01.07.2025
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| Subjects | |
| Online Access | Get full text |
| ISSN | 1229-5949 1229-5949 |
| DOI | 10.1002/bkcs.70036 |
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| Abstract | 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. |
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| AbstractList | 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. |
| Author | Lee, Jung Ho Lee, Jaeseok |
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| SubjectTerms | dynamic protein interactions fuzzy interactions intrinsically disordered proteins NMR spectroscopy protein–protein interactions |
| Title | Dynamic protein interactions probed by NMR spectroscopy |
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