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Terahertz radiation induces non-thermal structural changes associated with Fröhlich condensation in a protein crystal

Whether long-range quantum coherent states could exist in biological systems, and beyond low-temperature regimes where quantum physics is known to be applicable, has been the subject to debate for decades. It was proposed by Fröhlich that vibrational modes within protein molecules can order and cond...

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Autores principales: Lundholm, Ida V., Rodilla, Helena, Wahlgren, Weixiao Y., Duelli, Annette, Bourenkov, Gleb, Vukusic, Josip, Friedman, Ran, Stake, Jan, Schneider, Thomas, Katona, Gergely
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Crystallographic Association 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4711649/
https://www.ncbi.nlm.nih.gov/pubmed/26798828
http://dx.doi.org/10.1063/1.4931825
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author Lundholm, Ida V.
Rodilla, Helena
Wahlgren, Weixiao Y.
Duelli, Annette
Bourenkov, Gleb
Vukusic, Josip
Friedman, Ran
Stake, Jan
Schneider, Thomas
Katona, Gergely
author_facet Lundholm, Ida V.
Rodilla, Helena
Wahlgren, Weixiao Y.
Duelli, Annette
Bourenkov, Gleb
Vukusic, Josip
Friedman, Ran
Stake, Jan
Schneider, Thomas
Katona, Gergely
author_sort Lundholm, Ida V.
collection PubMed
description Whether long-range quantum coherent states could exist in biological systems, and beyond low-temperature regimes where quantum physics is known to be applicable, has been the subject to debate for decades. It was proposed by Fröhlich that vibrational modes within protein molecules can order and condense into a lowest-frequency vibrational mode in a process similar to Bose-Einstein condensation, and thus that macroscopic coherence could potentially be observed in biological systems. Despite the prediction of these so-called Fröhlich condensates almost five decades ago, experimental evidence thereof has been lacking. Here, we present the first experimental observation of Fröhlich condensation in a protein structure. To that end, and to overcome the challenges associated with probing low-frequency molecular vibrations in proteins (which has hampered understanding of their role in proteins' function), we combined terahertz techniques with a highly sensitive X-ray crystallographic method to visualize low-frequency vibrational modes in the protein structure of hen-egg white lysozyme. We found that 0.4 THz electromagnetic radiation induces non-thermal changes in electron density. In particular, we observed a local increase of electron density in a long α-helix motif consistent with a subtle longitudinal compression of the helix. These observed electron density changes occur at a low absorption rate indicating that thermalization of terahertz photons happens on a micro- to milli-second time scale, which is much slower than the expected nanosecond time scale due to damping of delocalized low frequency vibrations. Our analyses show that the micro- to milli-second lifetime of the vibration can only be explained by Fröhlich condensation, a phenomenon predicted almost half a century ago, yet never experimentally confirmed.
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spelling pubmed-47116492016-01-21 Terahertz radiation induces non-thermal structural changes associated with Fröhlich condensation in a protein crystal Lundholm, Ida V. Rodilla, Helena Wahlgren, Weixiao Y. Duelli, Annette Bourenkov, Gleb Vukusic, Josip Friedman, Ran Stake, Jan Schneider, Thomas Katona, Gergely Struct Dyn ARTICLES Whether long-range quantum coherent states could exist in biological systems, and beyond low-temperature regimes where quantum physics is known to be applicable, has been the subject to debate for decades. It was proposed by Fröhlich that vibrational modes within protein molecules can order and condense into a lowest-frequency vibrational mode in a process similar to Bose-Einstein condensation, and thus that macroscopic coherence could potentially be observed in biological systems. Despite the prediction of these so-called Fröhlich condensates almost five decades ago, experimental evidence thereof has been lacking. Here, we present the first experimental observation of Fröhlich condensation in a protein structure. To that end, and to overcome the challenges associated with probing low-frequency molecular vibrations in proteins (which has hampered understanding of their role in proteins' function), we combined terahertz techniques with a highly sensitive X-ray crystallographic method to visualize low-frequency vibrational modes in the protein structure of hen-egg white lysozyme. We found that 0.4 THz electromagnetic radiation induces non-thermal changes in electron density. In particular, we observed a local increase of electron density in a long α-helix motif consistent with a subtle longitudinal compression of the helix. These observed electron density changes occur at a low absorption rate indicating that thermalization of terahertz photons happens on a micro- to milli-second time scale, which is much slower than the expected nanosecond time scale due to damping of delocalized low frequency vibrations. Our analyses show that the micro- to milli-second lifetime of the vibration can only be explained by Fröhlich condensation, a phenomenon predicted almost half a century ago, yet never experimentally confirmed. American Crystallographic Association 2015-10-13 /pmc/articles/PMC4711649/ /pubmed/26798828 http://dx.doi.org/10.1063/1.4931825 Text en © 2015 Author(s). 2329-7778/2015/2(5)/054702/12 All article content, except where otherwise noted, is licensed under a Creative Commons Attribution 3.0 Unported License.
spellingShingle ARTICLES
Lundholm, Ida V.
Rodilla, Helena
Wahlgren, Weixiao Y.
Duelli, Annette
Bourenkov, Gleb
Vukusic, Josip
Friedman, Ran
Stake, Jan
Schneider, Thomas
Katona, Gergely
Terahertz radiation induces non-thermal structural changes associated with Fröhlich condensation in a protein crystal
title Terahertz radiation induces non-thermal structural changes associated with Fröhlich condensation in a protein crystal
title_full Terahertz radiation induces non-thermal structural changes associated with Fröhlich condensation in a protein crystal
title_fullStr Terahertz radiation induces non-thermal structural changes associated with Fröhlich condensation in a protein crystal
title_full_unstemmed Terahertz radiation induces non-thermal structural changes associated with Fröhlich condensation in a protein crystal
title_short Terahertz radiation induces non-thermal structural changes associated with Fröhlich condensation in a protein crystal
title_sort terahertz radiation induces non-thermal structural changes associated with fröhlich condensation in a protein crystal
topic ARTICLES
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4711649/
https://www.ncbi.nlm.nih.gov/pubmed/26798828
http://dx.doi.org/10.1063/1.4931825
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