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Electric-field-stimulated protein mechanics

Author

Listed:
  • Doeke R. Hekstra

    (Green Center for Systems Biology, UT Southwestern Medical Center
    † Present address: Department of Molecular and Cellular Biology and School of Engineering and Applied Sciences, Harvard University, 52 Oxford Street, Cambridge, Massachusetts 02138, USA.)

  • K. Ian White

    (Green Center for Systems Biology, UT Southwestern Medical Center)

  • Michael A. Socolich

    (Green Center for Systems Biology, UT Southwestern Medical Center)

  • Robert W. Henning

    (Center for Advanced Radiation Sources, The University of Chicago)

  • Vukica Šrajer

    (Center for Advanced Radiation Sources, The University of Chicago)

  • Rama Ranganathan

    (Green Center for Systems Biology, UT Southwestern Medical Center
    UT Southwestern Medical Center)

Abstract

The internal mechanics of proteins—the coordinated motions of amino acids and the pattern of forces constraining these motions—connects protein structure to function. Here we describe a new method combining the application of strong electric field pulses to protein crystals with time-resolved X-ray crystallography to observe conformational changes in spatial and temporal detail. Using a human PDZ domain (LNX2PDZ2) as a model system, we show that protein crystals tolerate electric field pulses strong enough to drive concerted motions on the sub-microsecond timescale. The induced motions are subtle, involve diverse physical mechanisms, and occur throughout the protein structure. The global pattern of electric-field-induced motions is consistent with both local and allosteric conformational changes naturally induced by ligand binding, including at conserved functional sites in the PDZ domain family. This work lays the foundation for comprehensive experimental study of the mechanical basis of protein function.

Suggested Citation

  • Doeke R. Hekstra & K. Ian White & Michael A. Socolich & Robert W. Henning & Vukica Šrajer & Rama Ranganathan, 2016. "Electric-field-stimulated protein mechanics," Nature, Nature, vol. 540(7633), pages 400-405, December.
    • Handle: RePEc:nat:nature:v:540:y:2016:i:7633:d:10.1038_nature20571
    DOI: 10.1038/nature20571
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    Cited by:

    1. Fanjun Li & Monifa A. Fahie & Kaitlyn M. Gilliam & Ryan Pham & Min Chen, 2022. "Mapping the conformational energy landscape of Abl kinase using ClyA nanopore tweezers," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    2. Eugene Klyshko & Justin Sung-Ho Kim & Lauren McGough & Victoria Valeeva & Ethan Lee & Rama Ranganathan & Sarah Rauscher, 2024. "Functional protein dynamics in a crystal," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    3. Yanghang Pan & Xinzhu Wang & Weiyang Zhang & Lingyu Tang & Zhangyan Mu & Cheng Liu & Bailin Tian & Muchun Fei & Yamei Sun & Huanhuan Su & Libo Gao & Peng Wang & Xiangfeng Duan & Jing Ma & Mengning Din, 2022. "Boosting the performance of single-atom catalysts via external electric field polarization," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    4. Kevin M. Dalton & Jack B. Greisman & Doeke R. Hekstra, 2022. "A unifying Bayesian framework for merging X-ray diffraction data," Nature Communications, Nature, vol. 13(1), pages 1-13, December.

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