<?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%">McKinney, J. A.</style></author><author><style face="normal" font="default" size="100%">Sharma, A.</style></author><author><style face="normal" font="default" size="100%">Crossen, K.</style></author><author><style face="normal" font="default" size="100%">Deng, Y.</style></author><author><style face="normal" font="default" size="100%">George, D. K.</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. G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Evidence of Intramolecular Structural Stabilization in Light Activated State of Orange Carotenoid Protein</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%">2020</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%">118</style></volume><pages><style face="normal" font="default" size="100%">208A-208A</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;p style=&quot;text-align: justify;&quot;&gt;Orange carotenoid protein (OCP) controls efficiency of the light harvesting antenna, the phycobilisome (PBS), in diverse cyanobacteria and prevents oxidative damage. It is the only known photoactive protein that uses a carotenoid, canthaxanthin, as its chromophore. The structure of OCP consists of two globular domains, connected by an unstructured loop, that forms a hydrophobic pocket for the carotenoid. In low light, canthaxanthin bound OCP is inactive and appears orange. Illumination by strong light results in an active state that interacts with the PBS to induce fluorescence quenching, a red appearance and conformational changes that include a 12Å shift by canthaxanthin into the N-terminal domain. Terahertz (THz) dynamical transition measurements and anisotropic terahertz microscopy are used to measure the intramolecular structural dynamics in the inactive and active states, which can be induced by photoexcitation or chaotropic salts. The measurements indicate that the active state has a decrease in structural flexibility, which may be related to enhanced interactions with the PBS.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><work-type><style face="normal" font="default" size="100%">Meeting Abstract</style></work-type><accession-num><style face="normal" font="default" size="100%">WOS:000513023201290</style></accession-num><notes><style face="normal" font="default" size="100%">ISI Document Delivery No.: KK8YX&lt;br/&gt;Times Cited: 0&lt;br/&gt;Cited Reference Count: 0&lt;br/&gt;McKinney, Jeffrey A. Sharma, Akansha Crossen, Kimberly Deng, Yanting George, Deepu K. Lechno-Yossef, Sigal Kerfeld, Cheryl Markelz, Andrea G.&lt;br/&gt;64th Annual Meeting of the Biophysical-Society&lt;br/&gt;Feb 15-19, 2020&lt;br/&gt;San Diego, CA&lt;br/&gt;Biophys Soc&lt;br/&gt;NSFNational Science Foundation (NSF) [DBI 1556359, MCB 1616529]; DOEUnited States Department of Energy (DOE) [DE-SC0016317]; NIH STTRUnited States Department of Health &amp; Human ServicesNational Institutes of Health (NIH) - USA [R41 GM125486]&lt;br/&gt;This work is supported by NSF grants DBI 1556359 and MCB 1616529, DOE grant DE-SC0016317 and NIH STTR R41 GM125486.&lt;br/&gt;&lt;br/&gt;1&lt;br/&gt;2&lt;br/&gt;Cell press&lt;br/&gt;Cambridge&lt;br/&gt;1542-0086</style></notes><auth-address><style face="normal" font="default" size="100%">[McKinney, Jeffrey A.|Sharma, Akansha|Crossen, Kimberly|Deng, Yanting|George, Deepu K.|Markelz, Andrea G.] SUNY Buffalo, Dept Phys, Buffalo, NY USA. [Lechno-Yossef, Sigal] Michigan State Univ, Dept Phys, E Lansing, MI 48824 USA. [Kerfeld, Cheryl] Michigan State Univ, Lawrence Berkeley Natl Lab LBNL, E Lansing, MI 48824 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%">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;
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