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Optical measurements of long-range protein vibrations

Author

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  • Gheorghe Acbas

    (University at Buffalo, SUNY)

  • Katherine A. Niessen

    (University at Buffalo, SUNY)

  • Edward H. Snell

    (Hauptman-Woodward Medical Research Institute, University at Buffalo, SUNY)

  • A.G. Markelz

    (University at Buffalo, SUNY
    Hauptman-Woodward Medical Research Institute, University at Buffalo, SUNY)

Abstract

Protein biological function depends on structural flexibility and change. From cellular communication through membrane ion channels to oxygen uptake and delivery by haemoglobin, structural changes are critical. It has been suggested that vibrations that extend through the protein play a crucial role in controlling these structural changes. While nature may utilize such long-range vibrations for optimization of biological processes, bench-top characterization of these extended structural motions for engineered biochemistry has been elusive. Here we show the first optical observation of long-range protein vibrational modes. This is achieved by orientation-sensitive terahertz near-field microscopy measurements of chicken egg white lysozyme single crystals. Underdamped modes are found to exist for frequencies >10 cm−1. The existence of these persisting motions indicates that damping and intermode coupling are weaker than previously assumed. The methodology developed permits protein engineering based on dynamical network optimization.

Suggested Citation

  • Gheorghe Acbas & Katherine A. Niessen & Edward H. Snell & A.G. Markelz, 2014. "Optical measurements of long-range protein vibrations," Nature Communications, Nature, vol. 5(1), pages 1-7, May.
  • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4076
    DOI: 10.1038/ncomms4076
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    Cited by:

    1. Félix-Martínez, G.J. & Picones, A. & Godínez-Fernández, J.R., 2024. "Short and long-range correlations in single-channel currents from inwardly rectifying K+ channels," Chaos, Solitons & Fractals, Elsevier, vol. 178(C).

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