TY - JOUR T1 - Blue Shift of a Molecular Crystal Phonon at the Solid to Liquid Phase Transition JF - Bulletin of the American Physical Society Y1 - 2019 A1 - Davie, Alex A1 - Vandrevala, Farah A1 - Deng, Yanting A1 - George, D. A1 - Sylvester, Eric D. A1 - Korter, T. A1 - Einarsson, E. A1 - Benedict, Jason B. A1 - Markelz, Andrea VL - 2019 ER - TY - CONF T1 - The Role of Dynamical Transition in Protein Function: Coupling of Protein Collective Vibrations and Water Dynamics T2 - 30th Anniversary Symposium of The Protein Society Y1 - 2016 A1 - Xu, Mengyang A1 - Niessen, Katherine A1 - Deng, Yanting A1 - Michki, Nigel A1 - Snell, Edward A1 - Markelz, Andrea AB -

Computational simulations have revealed protein collective vibrations prompt structural rearrangements to accomplish biological function. However, the biological importance of collective vibrations has not been experimentally demonstrated. The attempts have been hampered by the inability to distinguish localized water or side-chain relaxational motions from protein long-range vibrations using conventional techniques. The dynamical transition (DT), extensively observed using X-ray, neutron scattering, NMR and terahertz techniques [1,2], describes a rapid increase in the temperature-dependent dynamics of critically hydrated proteins above ∼220 K, and has been attributed to thermally activated solvent motions. While some proteins lose function below the specific temperature, others do not. We suggest the difference arises from the nature of the required motions for function. Specifically, functional motions enabled by long-range vibrations will be vulnerable to DT, which require surrounding solvent to be sufficiently mobile. We explored the coupling of protein vibrations to solvent dynamics by applying a recently developed technique, anisotropy terahertz microscopy [3], to directly measure the collective vibrations for lysozyme and investigate the temperature dependence in 150-300 K range. We find long-range intramolecular vibrations occur at 220K and rapidly increase in strength with increasing temperature, consistent with enhanced access above the DT. The results suggest collective vibrations are slaved to DT, and those proteins with function reliant on these motions will cease function below DT.

1. Doster,W., et al. Phys.Rev.Lett., 2010.104(9):098101.

2. Niessen,K., et al. Biophys.Rev., 2015.7,201.

3. Acbas,G., et al. Nat.Commun., 2014.5,3076.

JF - 30th Anniversary Symposium of The Protein Society CY - Baltimore, MD UR - https://onlinelibrary.wiley.com/doi/10.1002/pro.3026 ER - TY - JOUR T1 - Hydration dependence of conformational dielectric relaxation of lysozyme JF - Biophysical Journal Y1 - 2006 A1 - Knab, Joseph A1 - Chen, Jing-Yin A1 - Markelz, Andrea VL - 90 SN - 0006-3495 ER - TY - Generic T1 - Critical hydration and temperature effects on terahertz biomolecular sensing T2 - Chemical and Biological Standoff Detection III Y1 - 2005 A1 - Knab, Joseph A1 - Shah, Binni A1 - Chen, Jing-Yin A1 - Markelz, Andrea JF - Chemical and Biological Standoff Detection III PB - International Society for Optics and Photonics VL - 5995 ER - TY - JOUR T1 - THz time domain spectroscopy of biomolecular conformational modes JF - Physics in Medicine & Biology Y1 - 2002 A1 - Markelz, Andrea A1 - Whitmire, Scott A1 - Hillebrecht, Jay A1 - Birge, Robert VL - 47 SN - 0031-9155 ER - TY - Generic T1 - Terahertz grid frequency doublers T2 - Proc. Sixth Intl. Symp. Space Terahertz Tech Y1 - 1995 A1 - Chiao, Jung-Chih A1 - Markelz, Andrea A1 - Li, Yongjun A1 - Hacker, Jonathan A1 - Crowe, Thomas A1 - Allen, James A1 - Rutledge, David JF - Proc. Sixth Intl. Symp. Space Terahertz Tech PB - Citeseer UR - https://www.nrao.edu/meetings/isstt/papers/1995/1995199206.pdf ER -