TY - CONF T1 - Rapid Terahertz Dichroism Near Field Microscopy for Biomolecular Intramolecular Vibrational Spectroscopy T2 - APS 2018 Y1 - 2018 A1 - Deng, Y. A1 - Niessen, K. A1 - Markelz, A. JF - APS 2018 VL - A50.008 UR - http://meetings.aps.org/link/BAPS.2018.MAR.A50.8 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 - Generic T1 - The role of the protein surface on the local biological water dynamics T2 - Biosensing Ii Y1 - 2009 A1 - Liang, W. A1 - He, Y. F. A1 - George, D. A1 - Markelz, A. G. ED - Razeghi, M. ED - Mohseni, H. KW - alanine KW - dynamics KW - hydration KW - lysine KW - lysozyme KW - proteins KW - relaxation KW - spectroscopy KW - Terahertz KW - thz AB -

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's own structural dynamics. We discuss measurements of the THz absorption of water in the presence of hydrophilic and hydrophobic surfaces.

JF - Biosensing Ii T3 - Proceedings of SPIE PB - Spie-Int Soc Optical Engineering CY - Bellingham VL - 7397 SN - 978-0-8194-7687-6 N1 - ISI Document Delivery No.: BVQ85
Times Cited: 0
Cited Reference Count: 12
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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 ER - TY - Generic T1 - The role of structure in the protein dynamical transition T2 - 2008 33rd International Conference on Infrared, Millimeter and Terahertz Waves Y1 - 2008 A1 - He, Yunfen A1 - Markelz, Andrea G JF - 2008 33rd International Conference on Infrared, Millimeter and Terahertz Waves PB - IEEE SN - 1424421195 ER - TY - JOUR T1 - Relaxation times in InAs/AlSb quantum wells JF - Applied Physics Letters Y1 - 1998 A1 - Markelz, A. G. A1 - Asmar, N. G. A1 - Gwinn, E. G. VL - 72 UR - https://aip.scitation.org/doi/abs/10.1063/1.121377 ER - TY - JOUR T1 - RESONANT-ENERGY RELAXATION OF TERAHERTZ-DRIVEN 2-DIMENSIONAL ELECTRON GASES JF - Physical Review B Y1 - 1995 A1 - Asmar, N. G. A1 - Markelz, A. G. A1 - Gwinn, E. G. A1 - Cerne, J. A1 - Sherwin, M. S. A1 - Campman, K. L. A1 - Hopkins, P. F. A1 - Gossard, A. C. VL - 51 SN - 0163-1829 N1 - Sherwin, Mark S/Q-4762-2017
Sherwin, Mark S/0000-0002-3869-1893; Markelz, Andrea/0000-0003-0443-4319
119 ER -