00451nas a2200121 4500008004100000245010900041210006900150490001200219100001300231700001600244700001600260856005300276 2018 eng d00aRapid Terahertz Dichroism Near Field Microscopy for Biomolecular Intramolecular Vibrational Spectroscopy0 aRapid Terahertz Dichroism Near Field Microscopy for Biomolecular0 vA50.0081 aDeng, Y.1 aNiessen, K.1 aMarkelz, A. uhttp://meetings.aps.org/link/BAPS.2018.MAR.A50.802427nas a2200169 4500008004100000245012000041210006900161260001800230520183800248100001702086700002302103700001802126700001802144700001802162700002002180856005702200 2016 eng d00a The Role of Dynamical Transition in Protein Function: Coupling of Protein Collective Vibrations and Water Dynamics0 aRole of Dynamical Transition in Protein Function Coupling of Pro aBaltimore, MD3 a
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.
1 aXu, Mengyang1 aNiessen, Katherine1 aDeng, Yanting1 aMichki, Nigel1 aSnell, Edward1 aMarkelz, Andrea uhttps://onlinelibrary.wiley.com/doi/10.1002/pro.302601243nas a2200313 4500008004500000020002200045245007500067210006900142260004900211490000900260520038500269653001200654653001300666653001400679653001100693653001300704653001300717653001500730653001700745653001400762653000800776100001400784700001500798700001500813700002000828700001600848700001600864856004900880 2009 Engldsh a978-0-8194-7687-600aThe role of the protein surface on the local biological water dynamics0 arole of the protein surface on the local biological water dynami aBellinghambSpie-Int Soc Optical Engineering0 v73973 aProtein 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.
10aalanine10adynamics10ahydration10alysine10alysozyme10aproteins10arelaxation10aspectroscopy10aTerahertz10athz1 aLiang, W.1 aHe, Y., F.1 aGeorge, D.1 aMarkelz, A., G.1 aRazeghi, M.1 aMohseni, H. uhttps://markelz.physics.buffalo.edu/node/23200414nas a2200133 4500008004100000020001500041245006200056210005800118260000900176300000800185100001500193700002300208856004900231 2008 eng d a142442119500aThe role of structure in the protein dynamical transition0 arole of structure in the protein dynamical transition bIEEE a1-31 aHe, Yunfen1 aMarkelz, Andrea, G uhttps://markelz.physics.buffalo.edu/node/18800377nas a2200121 4500008004100000245004900041210004700090490000700137100002000144700001800164700001800182856005500200 1998 eng d00aRelaxation times in InAs/AlSb quantum wells 0 aRelaxation times in InAsAlSb quantum wells0 v721 aMarkelz, A., G.1 aAsmar, N., G.1 aGwinn, E., G. uhttps://aip.scitation.org/doi/abs/10.1063/1.12137700655nas a2200217 4500008004100000020001400041245008000055210006900135260001100204300001600215490000700231100001800238700002000256700001800276700001400294700002000308700002000328700002000348700002000368856004900388 1995 eng d a0163-182900aRESONANT-ENERGY RELAXATION OF TERAHERTZ-DRIVEN 2-DIMENSIONAL ELECTRON GASES0 aRESONANTENERGY RELAXATION OF TERAHERTZDRIVEN 2DIMENSIONAL ELECTR cJun 15 a18041-180440 v511 aAsmar, N., G.1 aMarkelz, A., G.1 aGwinn, E., G.1 aCerne, J.1 aSherwin, M., S.1 aCampman, K., L.1 aHopkins, P., F.1 aGossard, A., C. uhttps://markelz.physics.buffalo.edu/node/259