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Did we just capture Fröhlichs condensate? A study of quantum mechanical properties of proteins.

Image: National Institute of Standards and Technology, public domain, via Wikimedia Commons (licence). Cropped and resized. Image credits
  • Swedish Research Council
  • 1 Jan 2015 to 31 Dec 2015

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Project funded by Swedish Research Council (Project grant), grant 2014-04168_VR. Participating organisations named by the source: University of Gothenburg. Funded amount: SEK 400,000, as stated by the source. Runs 2015-01-01 to 2015-12-31. Keywords: Naturvetenskap, Natural Sciences, Fysik, Physical Sciences, Atom- och molekylfysik och optik, Atom and Molecular Physics and Optics. Source: OpenAIRE Graph, from the funder's project data (collected by OpenAIRE on 2025-12-04); national funding data, not CORDIS. Abstract given by the source: In 1968 Herbert Fröhlich predicted that strongly coupled oscillators (for example in the form of hydrogen bond network) in biological giant molecules condense into a single low frequency mode when continuously supplied with energy. We recently irradiated protein crystals with THz radiation and observed structural changes that I cannot attribute to the effect of short lived, localized vibrations, X-ray radiation damage or temperature increase. In this research proposal I want to explore how long these changes persist how far they spread in the crystal, how sensitive they are to the power of THz radiation. The combination of the emerging terahertz radiation technology and X-ray scattering techniques makes it possible to study very fundamental properties of proteins. THz excitation promises the induction of collective motions of atoms in proteins, because many domain and other collective motions within proteins happen on the picosecond timescale. X-ray crystallography on the other hand are sensitive structural probes to detect global and local structural changes due to THz irradiation. In order to find out what functional consequences of steady state illumination have on proteins, the changes in enzyme kinetic parameters will be correlated to the structural changes.

Original source.

Source: OpenAIRE Graph: projects of national funders, OpenAIRE, from the project data of Swedish Research Council. Retrieved 2026-10-28. Licence: Creative Commons Attribution 4.0 (OpenAIRE Graph). Selected metadata, adapted presentation; the publisher's record is authoritative. No endorsement by the source is implied. Licence: Creative Commons Attribution 4.0 (CC BY 4.0).

AI-assisted summary: The project, funded by the Swedish Research Council with a grant of SEK 400,000, investigates the quantum mechanical properties of proteins, specifically exploring structural changes in protein crystals irradiated with THz radiation. It runs from January 1, 2015, to December 31, 2015. Suggested technology pillar: sensing. Generated by AI from the public source text; it may contain errors and the original source is authoritative.

Source: explore.openaire.eu · checked 28 Oct 2026 · AI-assisted summary