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Protein conformational dynamics dictate the binding affinity for a ligand

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  • Moon-Hyeong Seo

    (Korea Advanced Institute of Science and Technology)

  • Jeongbin Park

    (Seoul National University)

  • Eunkyung Kim

    (Korea Advanced Institute of Science and Technology)

  • Sungchul Hohng

    (Seoul National University
    Seoul National University
    National Center for Creative Research Initiatives, Seoul National University)

  • Hak-Sung Kim

    (Korea Advanced Institute of Science and Technology)

Abstract

Interactions between a protein and a ligand are essential to all biological processes. Binding and dissociation are the two fundamental steps of ligand–protein interactions, and determine the binding affinity. Intrinsic conformational dynamics of proteins have been suggested to play crucial roles in ligand binding and dissociation. Here, we demonstrate how protein dynamics dictate the binding and dissociation of a ligand through a single-molecule kinetic analysis for a series of maltose-binding protein mutants that have different intrinsic conformational dynamics and dissociation constants for maltose. Our results provide direct evidence that the ligand dissociation is determined by the intrinsic opening rate of the protein.

Suggested Citation

  • Moon-Hyeong Seo & Jeongbin Park & Eunkyung Kim & Sungchul Hohng & Hak-Sung Kim, 2014. "Protein conformational dynamics dictate the binding affinity for a ligand," Nature Communications, Nature, vol. 5(1), pages 1-7, September.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4724
    DOI: 10.1038/ncomms4724
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    Cited by:

    1. Benedikt T. Kuhn & Jonathan Zöller & Iwan Zimmermann & Tim Gemeinhardt & Dogukan H. Özkul & Julian D. Langer & Markus A. Seeger & Eric R. Geertsma, 2024. "Interdomain-linkers control conformational transitions in the SLC23 elevator transporter UraA," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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