<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Sharma, A.</style></author><author><style face="normal" font="default" size="100%">George, D. K.</style></author><author><style face="normal" font="default" size="100%">Crossen, K.</style></author><author><style face="normal" font="default" size="100%">McKinney, J.</style></author><author><style face="normal" font="default" size="100%">Kerfeld, C.</style></author><author><style face="normal" font="default" size="100%">Markelz, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Is the Protein Dynamical Transition useful?</style></title><secondary-title><style face="normal" font="default" size="100%">Biophysical Journal</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2020</style></year></dates><volume><style face="normal" font="default" size="100%">118</style></volume><language><style face="normal" font="default" size="100%">eng</style></language><issue><style face="normal" font="default" size="100%">3</style></issue><section><style face="normal" font="default" size="100%">521a</style></section></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>10</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">McKinney, J.</style></author><author><style face="normal" font="default" size="100%">Sharma, A.</style></author><author><style face="normal" font="default" size="100%">Deng, Y.</style></author><author><style face="normal" font="default" size="100%">George, D.</style></author><author><style face="normal" font="default" size="100%">Lechno-Yossef, S.</style></author><author><style face="normal" font="default" size="100%">Kerfeld, C.</style></author><author><style face="normal" font="default" size="100%">Markelz, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Stabilization of Terahertz Vibrational Modes in Illuminated Orange Carotenoid Protein Crystals</style></title><secondary-title><style face="normal" font="default" size="100%">2020 45th International Conference on Infrared, Millimeter, and Terahertz Waves (IRMMW-THz)</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2020</style></year></dates><pub-location><style face="normal" font="default" size="100%">Buffalo, NY</style></pub-location><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p class=&quot;rtejustify&quot;&gt;Orange carotenoid protein (OCP) controls efficiency of the phycobilisome (PBS), the light harvesting antenna in cyanobacteria, to prevent oxidative damage. The OCP switches from resting state to photo protective state with intense blue light illumination. Questions persist as to why OCPR interaction increases with the PBS over that with the OCPO. Here we examine the role of long-range intramolecular vibrations within OCP. Using Stationary Sample Anisotropic Terahertz Microscopy (SSATM) we measure changes in the intramolecular vibrations with photo switching. We report the first observation of switching in the intramolecular vibrations with photoexcitation. Results suggest that there is a stiffening of the molecule in the photo protective state. This increase in structural stability may enhance the interaction with the PBS change in OCP interaction with PBS. In low light, carotenoid bound OCP appears orange (OCP &lt;sup&gt;o&lt;/sup&gt; ) and is inactive. Illumination by strong light converts OCP to the active, red (OCPR) state, which interacts with the PBS. A comparison of anisotropic THz microscopy measurements of dark adapted (OCP &lt;sup&gt;o&lt;/sup&gt; ) and illuminated OCP crystals indicate differences in their vibrational modes that may be important for OCP-PBS interactions.&lt;/p&gt;
</style></abstract></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>10</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">LaFave, T.</style></author><author><style face="normal" font="default" size="100%">Lee, A.</style></author><author><style face="normal" font="default" size="100%">Kao, T.-Y.</style></author><author><style face="normal" font="default" size="100%">Markelz, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">THz Transmission through Submillimeter Apertures</style></title><secondary-title><style face="normal" font="default" size="100%">IRMMW-THz</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2020</style></year><pub-dates><date><style  face="normal" font="default" size="100%">11/2020</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://ieeexplore.ieee.org/document/9370923</style></url></web-urls></urls><pub-location><style face="normal" font="default" size="100%">Buffalo NY</style></pub-location><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;div&gt;Terahertz near-field microspectroscopy is emerging as an essential tool for characterization of novel materials and biomolecules. It is important to ensure the near field geometry used does not introduce spectral artifacts. For example, many scanning techniques can be strongly influenced by the interaction between the scattering tip and the sample. Here we examine the spectroscopic effects of a 200 μm diameter aperture for THz near-field measurements. We use HFSS to model free-space transmission through samples with resonant absorbance as a function of sample thickness, lateral sample width, and aperture diameter. We examine the transmitted power and spectral fidelity for coupling of transmitted THz light onto a detector. These studies inform corrective post-measurement analysis algorithms and design of near-field detection systems.&lt;/div&gt;
</style></abstract></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Deng, Y. T.</style></author><author><style face="normal" font="default" size="100%">McKinney, J.</style></author><author><style face="normal" font="default" size="100%">Markelz, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Deuteration and Inhibitor Binding Dependence of Protein Collective Vibrations</style></title><secondary-title><style face="normal" font="default" size="100%">Biophysical Journal</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Biophys. J.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Biophysics</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2019</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Feb</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3</style></number><volume><style face="normal" font="default" size="100%">116</style></volume><pages><style face="normal" font="default" size="100%">488A-488A</style></pages><isbn><style face="normal" font="default" size="100%">0006-3495</style></isbn><language><style face="normal" font="default" size="100%">English</style></language><work-type><style face="normal" font="default" size="100%">Meeting Abstract</style></work-type><accession-num><style face="normal" font="default" size="100%">WOS:000460779802452</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: HO2XG&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 2&lt;br/&gt;Cited References: &lt;br/&gt;     Mahajan S, 2015, ARCH BIOCHEM BIOPHYS, V567, P59, DOI 10.1016/j.abb.2014.12.020&lt;br/&gt;     Niessen KA, 2017, BIOPHYS J, V112, P933, DOI 10.1016/j.bpj.2016.12.049&lt;br/&gt;Deng, Yanting Mckinney, Jeffrey Markelz, Andrea&lt;br/&gt;63rd Annual Meeting of the Biophysical-Society&lt;br/&gt;Mar 02-06, 2019&lt;br/&gt;Baltimore, MD&lt;br/&gt;Biophys Soc&lt;br/&gt;&lt;br/&gt;8&lt;br/&gt;Cell press&lt;br/&gt;Cambridge&lt;br/&gt;1542-0086&lt;br/&gt;1</style></notes><auth-address><style face="normal" font="default" size="100%">[Deng, Yanting|Mckinney, Jeffrey|Markelz, Andrea] SUNY Buffalo, Phys, Buffalo, NY USA.</style></auth-address></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">McKinney, J. A.</style></author><author><style face="normal" font="default" size="100%">Deng, Y. T.</style></author><author><style face="normal" font="default" size="100%">George, D.</style></author><author><style face="normal" font="default" size="100%">Markelz, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">The Effect of Crystal Contact Forces on the Protein Global Motions</style></title><secondary-title><style face="normal" font="default" size="100%">Biophysical Journal</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Biophys. J.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Biophysics</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2019</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Feb</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3</style></number><volume><style face="normal" font="default" size="100%">116</style></volume><pages><style face="normal" font="default" size="100%">489A-489A</style></pages><isbn><style face="normal" font="default" size="100%">0006-3495</style></isbn><language><style face="normal" font="default" size="100%">English</style></language><work-type><style face="normal" font="default" size="100%">Meeting Abstract</style></work-type><accession-num><style face="normal" font="default" size="100%">WOS:000460779802457</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: HO2XG&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 1&lt;br/&gt;Cited References: &lt;br/&gt;     Acbas G, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms4076&lt;br/&gt;McKinney, Jeffrey A. Deng, Yanting George, Deepu Markelz, Andrea&lt;br/&gt;63rd Annual Meeting of the Biophysical-Society&lt;br/&gt;Mar 02-06, 2019&lt;br/&gt;Baltimore, MD&lt;br/&gt;Biophys Soc&lt;br/&gt;&lt;br/&gt;8&lt;br/&gt;Cell press&lt;br/&gt;Cambridge&lt;br/&gt;1542-0086&lt;br/&gt;1</style></notes><auth-address><style face="normal" font="default" size="100%">[McKinney, Jeffrey A.|Deng, Yanting|George, Deepu|Markelz, Andrea] Univ Buffalo, Phys, Buffalo, NY USA.</style></auth-address></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Deng, Y. T.</style></author><author><style face="normal" font="default" size="100%">McKinney, J.</style></author><author><style face="normal" font="default" size="100%">Romo, T.</style></author><author><style face="normal" font="default" size="100%">Grossfield, A.</style></author><author><style face="normal" font="default" size="100%">Markelz, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Spectral Assignment of Lysozyme Collective Vibrations</style></title><secondary-title><style face="normal" font="default" size="100%">Biophysical Journal</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Biophys. J.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Biophysics</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2019</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Feb</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3</style></number><volume><style face="normal" font="default" size="100%">116</style></volume><pages><style face="normal" font="default" size="100%">564A-564A</style></pages><isbn><style face="normal" font="default" size="100%">0006-3495</style></isbn><language><style face="normal" font="default" size="100%">English</style></language><abstract><style face="normal" font="default" size="100%">&lt;div class=&quot;section-paragraph&quot;&gt;Global structural vibrations at terahertz (THz) frequencies have been associated with protein function and allosteric control. A chief obstacle to utilizing this control mechanism has been measurement of specific motions. Recently it was shown that while the vibrational density of states, and isotropic absorption spectra are broad and featureless, collective vibrations can be isolated based on their directionality using aligned samples (realized with protein crystals) and anisotropic THz microscopy [1]. However the assignment of resonant bands to specific structural motions was complicated by the high symmetry of the tetragonal crystals used, and the slow experimental method. To structurally map the vibrations of the chicken egg white lysozyme (CEWL) we measure anisotropic absorption of triclinic crystals using our new technique: ideal polarization varying anisotropic THz microscopy (IPV-ATM). The low symmetry triclinic crystals provide absolute protein orientation, and the near field IPV-ATM rapidly measures broadband terahertz linear dichroism of the microcrystals. All measurements were performed at room temperature under 100% humidity conditions. The unit cell parameters of triclinic lysozyme nitrate crystals, α = 28.5A°, b = 32.7A°, c = 35.1A°, α = 88.2°, β = 108.9°, γ = 111.9°, belonging to the P1 space group, were determined by X-ray diffraction before and after THz measurements. The intramolecular vibrational absorbance of the triclinic crystals has a more complex polarization dependence than the higher symmetry tetragonal crystals, as expected. While the tetragonal crystals have two strong bands at 45cm&lt;sup&gt;−1&lt;/sup&gt; and 55cm&lt;sup&gt;−1&lt;/sup&gt;, the triclinic crystals have a series of narrow bands between 40 and 60cm&lt;sup&gt;−1&lt;/sup&gt; and a prominent band at 30cm&lt;sup&gt;−1&lt;/sup&gt;. We compare the measured spectra to normal mode ensemble averaged calculations to assign the observed resonances, and isolating which collective motions impact the catalytic site.&lt;/div&gt;</style></abstract><work-type><style face="normal" font="default" size="100%">Meeting Abstract</style></work-type><accession-num><style face="normal" font="default" size="100%">WOS:000460779802832</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: HO2XG&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 1&lt;br/&gt;Cited References: &lt;br/&gt;     Niessen KA, 2017, BIOPHYS J, V112, P933, DOI 10.1016/j.bpj.2016.12.049&lt;br/&gt;Deng, Yanting Mckinney, Jeffrey Romo, Tod Grossfield, Alan Markelz, Andrea&lt;br/&gt;63rd Annual Meeting of the Biophysical-Society&lt;br/&gt;Mar 02-06, 2019&lt;br/&gt;Baltimore, MD&lt;br/&gt;Biophys Soc&lt;br/&gt;&lt;br/&gt;8&lt;br/&gt;Cell press&lt;br/&gt;Cambridge&lt;br/&gt;1542-0086&lt;br/&gt;1</style></notes><auth-address><style face="normal" font="default" size="100%">[Deng, Yanting|Mckinney, Jeffrey|Markelz, Andrea] SUNY Buffalo, Phys, Buffalo, NY USA. [Romo, Tod|Grossfield, Alan] Univ Rochester, Med Ctr, Dept Biochem &amp; Biophys, Rochester, NY 14642 USA.</style></auth-address></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>47</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Luck, C.</style></author><author><style face="normal" font="default" size="100%">Xu, M.</style></author><author><style face="normal" font="default" size="100%">Markelz, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Investigation of the Isotope Shift in Protein Collective Vibrations</style></title><secondary-title><style face="normal" font="default" size="100%">APS 2018</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2018</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://meetings.aps.org/link/BAPS.2018.MAR.A50.13</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">A50.013</style></volume><language><style face="normal" font="default" size="100%">eng</style></language></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>47</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Xu, M.</style></author><author><style face="normal" font="default" size="100%">Deng, Y.</style></author><author><style face="normal" font="default" size="100%">Luck, C.</style></author><author><style face="normal" font="default" size="100%">Sharma, A.</style></author><author><style face="normal" font="default" size="100%">Markelz, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Measuring Protein Intramolecular Dynamics with Terahertz Light: Functional Changes and Relevance to Biology</style></title><secondary-title><style face="normal" font="default" size="100%">APS 2018</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2018</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://meetings.aps.org/link/BAPS.2018.MAR.H50.1</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">H50.001</style></volume><language><style face="normal" font="default" size="100%">eng</style></language></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>47</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Deng, Y.</style></author><author><style face="normal" font="default" size="100%">Niessen, K.</style></author><author><style face="normal" font="default" size="100%">Markelz, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Rapid Terahertz Dichroism Near Field Microscopy for Biomolecular Intramolecular Vibrational Spectroscopy</style></title><secondary-title><style face="normal" font="default" size="100%">APS 2018</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2018</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://meetings.aps.org/link/BAPS.2018.MAR.A50.8</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">A50.008</style></volume><language><style face="normal" font="default" size="100%">eng</style></language></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>47</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Deng, Y.</style></author><author><style face="normal" font="default" size="100%">Xu, M.</style></author><author><style face="normal" font="default" size="100%">Liu, H.</style></author><author><style face="normal" font="default" size="100%">Blankenship, R.</style></author><author><style face="normal" font="default" size="100%">Markelz, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Global Picosecond Structural Dynamics of Orange Carotenoid Protein in Photo/Chemical Activated Signaling States</style></title><secondary-title><style face="normal" font="default" size="100%">APS 2017 S4.002</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2017</style></year><pub-dates><date><style  face="normal" font="default" size="100%">03/2017</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://meetings.aps.org/link/BAPS.2017.MAR.S4.2</style></url></web-urls></urls><language><style face="normal" font="default" size="100%">eng</style></language></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>47</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Xu, M.</style></author><author><style face="normal" font="default" size="100%">Myles, D.</style></author><author><style face="normal" font="default" size="100%">Blankenship, R.</style></author><author><style face="normal" font="default" size="100%">Markelz, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Temperature dependence of phonons in photosynthesis proteins</style></title><secondary-title><style face="normal" font="default" size="100%">APS 2017 S4.003</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2017</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://meetings.aps.org/link/BAPS.2017.MAR.S4.3</style></url></web-urls></urls><language><style face="normal" font="default" size="100%">eng</style></language></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Ye, S. J.</style></author><author><style face="normal" font="default" size="100%">Markelz, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Hydration Effects on Energy Relaxation of Ferric Cytochrome C Films after Soret-Band Photoexcitation</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Physical Chemistry B</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Phys. Chem. B</style></alt-title><short-title><style face="normal" font="default" size="100%">J. Phys. Chem. BJ. Phys. Chem. B</style></short-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">circular-dichroism</style></keyword><keyword><style  face="normal" font="default" size="100%">conformation change</style></keyword><keyword><style  face="normal" font="default" size="100%">dynamics</style></keyword><keyword><style  face="normal" font="default" size="100%">ferricytochrome-c</style></keyword><keyword><style  face="normal" font="default" size="100%">protein hydration</style></keyword><keyword><style  face="normal" font="default" size="100%">resolved resonance raman</style></keyword><keyword><style  face="normal" font="default" size="100%">spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">unfolded states</style></keyword><keyword><style  face="normal" font="default" size="100%">vibrational-relaxation</style></keyword><keyword><style  face="normal" font="default" size="100%">water-molecules</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2010</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Nov</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">46</style></number><volume><style face="normal" font="default" size="100%">114</style></volume><pages><style face="normal" font="default" size="100%">15151-15157</style></pages><isbn><style face="normal" font="default" size="100%">1520-6106</style></isbn><language><style face="normal" font="default" size="100%">English</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Protein hydration plays a critical role in protein dynamics and biological processes. Pump-probe transmission measurement has been applied to investigate the hydration effects on the energy relaxation of a heme protein ferric Cytochrome c (Cyt c) film after soret-band photoexcitation. Transient dynamics study indicates that the energy internal conversion time of similar to 300 fs is independent of hydration. The vibrationally excited electronic ground-state recovery rates show two transitions at the hydration level of h = 12.4-16.5% and 21.7-23.5%. The first transition occurs at the hydration level for the onset of an increasing ferric Cyt c flexibility while the second transition occurs at the saturated hydration level. The hydration dependence of steady-state electronic absorption spectrum results shows that the Q-band peak is nearly constant in center wavelength, but the line width surprisingly narrows with increasing hydration. For the similar to 695 nm absorbance associated with the MET80-Fe bond, the intensity increases with increasing hydration and slightly blue shifts. The 695 nm peak grows rapidly at h = 12.4% and then plateaus at h = 21.7%. This research shows that similar to 695 nm absorbance and ground-state recovery rates are sensitive to the hydration of the protein. This study will aid in understanding how hydration modulates the activity of the protein dynamics at a local level.&lt;/p&gt;</style></abstract><work-type><style face="normal" font="default" size="100%">Article</style></work-type><accession-num><style face="normal" font="default" size="100%">WOS:000284287700044</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: 681CT&lt;br/&gt;Times Cited: 3&lt;br/&gt;Cited Reference Count: 87&lt;br/&gt;Cited References: &lt;br/&gt;     Bagchi B, 2005, CHEM REV, V105, P3197, DOI 10.1021/cr020661+&lt;br/&gt;     BAI YW, 1995, SCIENCE, V269, P192, DOI 10.1126/science.7618079&lt;br/&gt;     Bertini I, 2000, J MAGN RESON, V147, P1, DOI 10.1006/jmre.2000.2131&lt;br/&gt;     Bizzarri AR, 2002, J PHYS CHEM B, V106, P6617, DOI 10.1021/jp020100m&lt;br/&gt;     BONE S, 1985, J MOL BIOL, V181, P323, DOI 10.1016/0022-2836(85)90096-8&lt;br/&gt;     Bone S, 2008, J PHYS CHEM B, V112, P10071, DOI 10.1021/jp8009782&lt;br/&gt;     BULL HB, 1968, ARCH BIOCHEM BIOPHYS, V128, P488, DOI 10.1016/0003-9861(68)90055-6&lt;br/&gt;     BULL HB, 1970, ARCH BIOCHEM BIOPHYS, V137, P299, DOI 10.1016/0003-9861(70)90443-1&lt;br/&gt;     CHAMPION PM, 1981, J CHEM PHYS, V75, P490, DOI 10.1063/1.441846&lt;br/&gt;     Chen EF, 1999, J AM CHEM SOC, V121, P3811, DOI 10.1021/ja983169+&lt;br/&gt;     Chen JY, 2005, PHYS REV E, V72, DOI 10.1103/PhysRevE.72.040901&lt;br/&gt;     Cianetti S, 2004, J AM CHEM SOC, V126, P13932, DOI 10.1021/ja046442i&lt;br/&gt;     Dragomir I, 2007, BIOPHYS J, V92, P989, DOI 10.1529/biophysj.106.095976&lt;br/&gt;     Eaton W A, 1981, Methods Enzymol, V76, P175&lt;br/&gt;     EATON WA, 1967, J CHEM PHYS, V46, P2533, DOI 10.1063/1.1841081&lt;br/&gt;     EATON WA, 1968, J CHEM PHYS, V49, P985, DOI 10.1063/1.1670263&lt;br/&gt;     Ehrler OT, 2009, ACCOUNTS CHEM RES, V42, P769, DOI 10.1021/ar800263z&lt;br/&gt;     FERRAND M, 1993, P NATL ACAD SCI USA, V90, P9668, DOI 10.1073/pnas.90.20.9668&lt;br/&gt;     GASCOYNE PRC, 1977, J CHEM SOC FARAD T 1, V73, P171, DOI 10.1039/f19777300171&lt;br/&gt;     GIBSON QH, 1957, NATURE, V180, P1416, DOI 10.1038/1801416b0&lt;br/&gt;     Gregory R.B., 1995, PROTEIN SOLVENT INTE&lt;br/&gt;     HALLE B, 1981, J AM CHEM SOC, V103, P500, DOI 10.1021/ja00393a004&lt;br/&gt;     Halle B, 2004, PHILOS T R SOC B, V359, P1207, DOI 10.1098/rstb.2004.1499&lt;br/&gt;     Henchman RH, 2002, PROTEIN SCI, V11, P2080, DOI 10.1110/ps.0214002&lt;br/&gt;     Hertel IV, 2006, REP PROG PHYS, V69, P1897, DOI 10.1088/0034-4885/69/6/R06&lt;br/&gt;     Jayaram B, 2004, ANNU REV BIOPH BIOM, V33, P343, DOI 10.1146/annurev.biophys.33.110502.140414&lt;br/&gt;     Jimenez R, 2002, J PHYS CHEM B, V106, P9172, DOI 10.1021/jp0209648&lt;br/&gt;     JONES CM, 1993, P NATL ACAD SCI USA, V90, P11860, DOI 10.1073/pnas.90.24.11860&lt;br/&gt;     Joti Y, 2008, BIOPHYS J, V94, P4435, DOI 10.1529/biophysj.107.118042&lt;br/&gt;     Jougeward K. 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[Markelz, Andrea] SUNY Buffalo, Dept Phys, Buffalo, NY 14260 USA.&lt;br/&gt;Ye, SJ (corresponding author), Univ Sci &amp; Technol China, Hefei Natl Lab Phys Sci Microscale, Hefei 230026, Anhui, Peoples R China.&lt;br/&gt;shujiye@ustc.edu.cn|amarkelz@buffalo.edu</style></auth-address></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Sherwin, M. S.</style></author><author><style face="normal" font="default" size="100%">Craig, K.</style></author><author><style face="normal" font="default" size="100%">Galdrikian, B.</style></author><author><style face="normal" font="default" size="100%">Heyman, J.</style></author><author><style face="normal" font="default" size="100%">Markelz, A.</style></author><author><style face="normal" font="default" size="100%">Campman, K.</style></author><author><style face="normal" font="default" size="100%">Fafard, S.</style></author><author><style face="normal" font="default" size="100%">Hopkins, P. F.</style></author><author><style face="normal" font="default" size="100%">Gossard, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">NONLINEAR QUANTUM DYNAMICS IN SEMICONDUCTOR QUANTUM-WELLS</style></title><secondary-title><style face="normal" font="default" size="100%">Physica D-Nonlinear Phenomena</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">1995</style></year><pub-dates><date><style  face="normal" font="default" size="100%">May 15</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">1-3</style></number><volume><style face="normal" font="default" size="100%">83</style></volume><pages><style face="normal" font="default" size="100%">229-242</style></pages><isbn><style face="normal" font="default" size="100%">0167-2789</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;We discuss recent measurements of the nonlinear response of electrons in wide quantum wells driven by intense electromagnetic radiation at terahertz frequencies. The theme is the interplay of quantum mechanics, strong periodic driving, the electron-electron interaction and dissipation. We discuss harmonic generation from an asymmetric double quantum well in which the effects of dynamic screening are important. Measurements and theory are found to be in good agreement. We also discuss intensity-dependent absorption in a 400 Angstrom square quantum well. A new nonlinear quantum effect occurs, in which the frequency at which electromagnetic radiation is absorbed shifts to the red with increasing intensity. The preliminary experimental results are in agreement with a theory by Zaluzny, in which the source of the nonlinearity is the self-consistent potential in the Hartree approximation for the electron dynamics.&lt;/p&gt;</style></abstract><accession-num><style face="normal" font="default" size="100%">WOS:A1995RA41200018</style></accession-num><notes><style face="normal" font="default" size="100%">Sherwin, Mark S/Q-4762-2017&lt;br/&gt;Sherwin, Mark S/0000-0002-3869-1893; Markelz, Andrea/0000-0003-0443-4319&lt;br/&gt;14th Annual International Conference of the Center-for-Nonlinear-Studies - Quantum Complexity in Mesoscopic Systems&lt;br/&gt;May 16-20, 1994&lt;br/&gt;Los alamos, nm&lt;br/&gt;Ctr nonlinear studies&lt;br/&gt;34</style></notes></record></records></xml>