00619nas a2200193 4500008004100000245008500041210006900126490000900195100001600204700002200220700001800242700001500260700002400275700001500299700001800314700002400332700002000356856004900376 2019 eng d00aBlue Shift of a Molecular Crystal Phonon at the Solid to Liquid Phase Transition0 aBlue Shift of a Molecular Crystal Phonon at the Solid to Liquid 0 v20191 aDavie, Alex1 aVandrevala, Farah1 aDeng, Yanting1 aGeorge, D.1 aSylvester, Eric, D.1 aKorter, T.1 aEinarsson, E.1 aBenedict, Jason, B.1 aMarkelz, Andrea uhttps://markelz.physics.buffalo.edu/node/27600510nas a2200157 4500008004100000245005500041210005500096260003100151300001200182100001800194700001700212700002600229700002500255700002300280856004900303 2018 eng d00aTerahertz Light Fingerprints Biomolecular Dynamics0 aTerahertz Light Fingerprints Biomolecular Dynamics bOptical Society of America aSW3D. 51 aDeng, Yanting1 aXu, Mengyang1 aNiessen, Katherine, A1 aGeorge, Deepu, Koshy1 aMarkelz, Andrea, G uhttps://markelz.physics.buffalo.edu/node/18200552nas a2200181 4500008004100000020001400041245006300055210006300118260001000181300001400191490000800205100002700213700001700240700001800257700002200275700002400297856004900321 2017 eng d a0006-349500aImportance of Protein Vibration Directionality on Function0 aImportance of Protein Vibration Directionality on Function cFeb 3 a353A-353A0 v1121 aNiessen, Katherine, A.1 aXu, Mengyang1 aDeng, Yanting1 aSnell, Edward, H.1 aMarkelz, Andrea, G. uhttps://markelz.physics.buffalo.edu/node/25402250nas a2200157 4500008004100000245009400041210006900135260001700204520170800221100001801929700001701947700002701964700002001991700002402011856005702035 2016 eng d00aDirect Measurements of the Long-Range Collective Vibrations of Photoactive Yellow Protein0 aDirect Measurements of the LongRange Collective Vibrations of Ph aBaltimore MD3 a
Long-range collective vibrations are thought to be crucial to protein functions. In the case of photoactive protein family, modeling suggests the intramolecular vibrations provide an efficient means of energy relaxation[1], feedback for enhancement of chromophore vibrations that promote structural transitions[2] and can assist in charge energy transfer[3]. As a paradigm of this family, photoactive yellow protein (PYP) is a cytoplasmic photocycling protein related to negative phototactic response to blue light in purple photosynthetic bacteria. PYP has a p-coumaric acid chromophore binding to the cysteine residue via a thioester bond, whose vibrations were found to overlap calculated vibrations of the protein scaffold. Using our unique technique of anisotropic terahertz microscopy(ATM)[4], we measure the intramolecular vibrations for PYP for the first time, including cycling between ground and blue shift (pB) states. Room temperature ATM measurements are performed in the dark and with continuous wave illumination at 488nm, resulting in a steady pB state with approximately 5% population conversion. In pB state, we find an overall decrease in the strength of resonant band in frequency range of 30-60 cm-1. Our calculated spectra using quasi-harmonic analysis indicate that our measurements are dominated by the protein vibrations, rather than the pCA chromophore, allowing us to characterize how the scaffold dynamics changes with functional states and mutations.
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2. Mataga, N., et al. Chem. Phys. Lett., 2002. 352(3-4): p. 220-225.
3. Fokas, A.S., et al. Photosynth. Res., 2014. 122
1 aDeng, Yanting1 aXu, Mengyang1 aNiessen, Katherine, A.1 aSchmidt, Marius1 aMarkelz, Andrea, G. uhttps://onlinelibrary.wiley.com/doi/10.1002/pro.302602427nas 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 aComputational 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.3026