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Correlation of membrane protein conformational and functional dynamics

Author

Listed:
  • Raghavendar Reddy Sanganna Gari

    (Weill Cornell Medicine, Department of Anesthesiology
    Weill Cornell Medicine, Department of Physiology and Biophysics)

  • Joel José Montalvo‐Acosta

    (Laboratoire International Associé CNRS and University of Illinois at Urbana-Champaign, Université de Lorraine)

  • George R. Heath

    (Weill Cornell Medicine, Department of Anesthesiology
    University of Leeds)

  • Yining Jiang

    (Weill Cornell Medicine, Department of Physiology and Biophysics)

  • Xiaolong Gao

    (Weill Cornell Medicine, Department of Anesthesiology)

  • Crina M. Nimigean

    (Weill Cornell Medicine, Department of Anesthesiology
    Weill Cornell Medicine, Department of Physiology and Biophysics)

  • Christophe Chipot

    (Laboratoire International Associé CNRS and University of Illinois at Urbana-Champaign, Université de Lorraine
    University of Illinois at Urbana-Champaign)

  • Simon Scheuring

    (Weill Cornell Medicine, Department of Anesthesiology
    Weill Cornell Medicine, Department of Physiology and Biophysics)

Abstract

Conformational changes in ion channels lead to gating of an ion-conductive pore. Ion flux has been measured with high temporal resolution by single-channel electrophysiology for decades. However, correlation between functional and conformational dynamics remained difficult, lacking experimental techniques to monitor sub-millisecond conformational changes. Here, we use the outer membrane protein G (OmpG) as a model system where loop-6 opens and closes the β-barrel pore like a lid in a pH-dependent manner. Functionally, single-channel electrophysiology shows that while closed states are favored at acidic pH and open states are favored at physiological pH, both states coexist and rapidly interchange in all conditions. Using HS-AFM height spectroscopy (HS-AFM-HS), we monitor sub-millisecond loop-6 conformational dynamics, and compare them to the functional dynamics from single-channel recordings, while MD simulations provide atomistic details and energy landscapes of the pH-dependent loop-6 fluctuations. HS-AFM-HS offers new opportunities to analyze conformational dynamics at timescales of domain and loop fluctuations.

Suggested Citation

  • Raghavendar Reddy Sanganna Gari & Joel José Montalvo‐Acosta & George R. Heath & Yining Jiang & Xiaolong Gao & Crina M. Nimigean & Christophe Chipot & Simon Scheuring, 2021. "Correlation of membrane protein conformational and functional dynamics," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-24660-1
    DOI: 10.1038/s41467-021-24660-1
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    Cited by:

    1. Yining Jiang & Zhaokun Wang & Simon Scheuring, 2025. "A structural biology compatible file format for atomic force microscopy," Nature Communications, Nature, vol. 16(1), pages 1-16, December.

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