Dynamical Transition in Dehydrated Proteins.
| Autor: | Kölbel J; Department of Chemical Engineering, University of Cambridge, Cambridge CB3 0AS, U.K., Anuschek ML; Department of Chemical Engineering, University of Cambridge, Cambridge CB3 0AS, U.K.; Department of Pharmacy - Center for Drug Research, Pharmaceutical Technology and Biopharmaceutics, Ludwig-Maximilians Universität, Butenandtstrasse 5, 81377 Munich, Germany., Stelzl I; Department of Pharmacy - Center for Drug Research, Pharmaceutical Technology and Biopharmaceutics, Ludwig-Maximilians Universität, Butenandtstrasse 5, 81377 Munich, Germany., Santitewagun S; Department of Chemical Engineering, University of Cambridge, Cambridge CB3 0AS, U.K., Friess W; Department of Pharmacy - Center for Drug Research, Pharmaceutical Technology and Biopharmaceutics, Ludwig-Maximilians Universität, Butenandtstrasse 5, 81377 Munich, Germany., Zeitler JA; Department of Chemical Engineering, University of Cambridge, Cambridge CB3 0AS, U.K. |
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| Jazyk: | angličtina |
| Zdroj: | The journal of physical chemistry letters [J Phys Chem Lett] 2024 Apr 04; Vol. 15 (13), pp. 3581-3590. Date of Electronic Publication: 2024 Mar 25. |
| DOI: | 10.1021/acs.jpclett.3c03584 |
| Abstrakt: | Terahertz time-domain spectroscopy and differential scanning calorimetry were used to study the role of the dynamics of biomolecules decoupled from solvent effects. Lyophilized sucrose exhibited steadily increasing absorption with temperature as anharmonic excitations commenced as the system emerged from a deep minimum of the potential energy landscape where harmonic vibrations dominate. The polypeptide bacitracin and two globular proteins, lysozyme and human serum albumin, showed a more complex temperature dependence. Further analysis focused on the spectral signature below and above the boson peak. We found evidence of the onset of anharmonic motions that are characteristic for partial unfolding and molecular jamming in the dry biomolecules. The activation of modes of the protein molecules at temperatures comparable to the protein dynamical transition temperature was observed in the absence of hydration. No evidence of Fröhlich coherence, postulated to facilitate biological function, was found in our experiments. |
| Databáze: | MEDLINE |
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