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Anisotropic energy flow and allosteric ligand binding in albumin

Author

Listed:
  • Guifeng Li

    (Emory University)

  • Donny Magana

    (Emory University)

  • R. Brian Dyer

    (Emory University)

Abstract

Allosteric interactions in proteins generally involve propagation of local structural changes through the protein to a remote site. Anisotropic energy transport is thought to couple the remote sites, but the nature of this process is poorly understood. Here, we report the relationship between energy flow through the structure of bovine serum albumin and allosteric interactions between remote ligand binding sites of the protein. Ultrafast infrared spectroscopy is used to probe the flow of energy through the protein backbone following excitation of a heater dye, a metalloporphyrin or malachite green, bound to different binding sites in the protein. We observe ballistic and anisotropic energy flow through the protein structure following input of thermal energy into the flexible ligand binding sites, without local heating of the rigid helix bundles that connect these sites. This efficient energy transport mechanism enables the allosteric propagation of binding energy through the connecting helix structures.

Suggested Citation

  • Guifeng Li & Donny Magana & R. Brian Dyer, 2014. "Anisotropic energy flow and allosteric ligand binding in albumin," Nature Communications, Nature, vol. 5(1), pages 1-7, May.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4100
    DOI: 10.1038/ncomms4100
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    Cited by:

    1. Livi, Lorenzo & Maiorino, Enrico & Pinna, Andrea & Sadeghian, Alireza & Rizzi, Antonello & Giuliani, Alessandro, 2016. "Analysis of heat kernel highlights the strongly modular and heat-preserving structure of proteins," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 441(C), pages 199-214.
    2. Maggi, Luca, 2021. "How super-localization affects vibrational energy exchange process in proteins," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 562(C).

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