@conference {285, title = {Rapid Terahertz Dichroism Near Field Microscopy for Biomolecular Intramolecular Vibrational Spectroscopy}, booktitle = {APS 2018}, volume = {A50.008}, year = {2018}, url = {http://meetings.aps.org/link/BAPS.2018.MAR.A50.8}, author = {Deng, Y. and Niessen, K. and Markelz, A.} } @conference {547, title = { The Role of Dynamical Transition in Protein Function: Coupling of Protein Collective Vibrations and Water Dynamics}, booktitle = {30th Anniversary Symposium of The Protein Society}, year = {2016}, address = {Baltimore, MD}, abstract = {

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.

}, doi = {10.1002/pro.3026}, url = {https://onlinelibrary.wiley.com/doi/10.1002/pro.3026}, author = {Xu, Mengyang and Niessen, Katherine and Deng, Yanting and Michki, Nigel and Snell, Edward and Markelz, Andrea} } @proceedings {232, title = {The role of the protein surface on the local biological water dynamics}, volume = {7397}, year = {2009}, note = {ISI Document Delivery No.: BVQ85
Times Cited: 0
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Liang, Wei He, Yunfen George, Deepu Markelz, A. G.
Proceedings Paper
Conference on Biosensing II
Aug 04-06, 2009
San Diego, CA
Spie
George, Deepu/J-9882-2014
George, Deepu/0000-0003-0021-0705; Markelz, Andrea/0000-0003-0443-4319
1000 20th st, po box 10, bellingham, wa 98227-0010 usa
0277-786x
73970t}, publisher = {Spie-Int Soc Optical Engineering}, address = {Bellingham}, abstract = {

Protein function is reliant on structural flexibility and this flexibility is slaved to the surrounding solvent. Here we discuss how the exposed surface of the protein influences the solvent dynamics and thereby influences the protein{\textquoteright}s own structural dynamics. We discuss measurements of the THz absorption of water in the presence of hydrophilic and hydrophobic surfaces.

}, keywords = {alanine, dynamics, hydration, lysine, lysozyme, proteins, relaxation, spectroscopy, Terahertz, thz}, isbn = {978-0-8194-7687-6}, doi = {https://doi.org/10.1117/12.828697}, author = {Liang, W. and He, Y. F. and George, D. and Markelz, A. G.}, editor = {Razeghi, M. and Mohseni, H.} } @proceedings {188, title = {The role of structure in the protein dynamical transition}, year = {2008}, pages = {1-3}, publisher = {IEEE}, isbn = {1424421195}, doi = {https://doi.org/10.1109/ICIMW.2008.4665800}, author = {He, Yunfen and Markelz, Andrea G} } @article {297, title = {Relaxation times in InAs/AlSb quantum wells }, journal = {Applied Physics Letters}, volume = {72}, year = {1998}, chapter = {2439}, doi = {10.1063/1.121377}, url = {https://aip.scitation.org/doi/abs/10.1063/1.121377}, author = {Markelz, A. G. and Asmar, N. G. and Gwinn, E. G.} } @article {259, title = {RESONANT-ENERGY RELAXATION OF TERAHERTZ-DRIVEN 2-DIMENSIONAL ELECTRON GASES}, journal = {Physical Review B}, volume = {51}, number = {24}, year = {1995}, note = {Sherwin, Mark S/Q-4762-2017
Sherwin, Mark S/0000-0002-3869-1893; Markelz, Andrea/0000-0003-0443-4319
119}, month = {Jun 15}, pages = {18041-18044}, isbn = {0163-1829}, doi = {10.1103/PhysRevB.51.18041}, author = {Asmar, N. G. and Markelz, A. G. and Gwinn, E. G. and Cerne, J. and Sherwin, M. S. and Campman, K. L. and Hopkins, P. F. and Gossard, A. C.} }