{"95251":{"#nid":"95251","#data":{"type":"event","title":"(0412) Dr. Clemence Corminboeuf, Univ of Georgia","body":[{"value":"\u003Cp\u003EDr. Clemence Corminboeuf, Center for Computational Chemistry, University of Georgia\n\u003C\/p\u003E\n\u003Cp\u003EThe role of electron delocalization in biology: A step by step adventure\n\u003C\/p\u003E\n\u003Cp\u003EElectron delocalization within molecules impacts considerably all areas of chemistry, and biochemistry in particular. For instance, inter- or intramolecular ring current effects can have drastic influences on NMR chemical shieldings in biological systems. Similarly, aromatic interactions are believed to play a crucial role in biological recognition and in protein activity.\u003Cbr \/\u003E\nQuantum chemistry provides a unique way for directly assessing the role of electron delocalization in biology. However, molecular property computations of biological systems are still far from routine. As a first step, I will describe a QM\/MM methodology, which allows for an accurate description of the geometrical and electronic structure of enzyme active sites, while properly including the effect of the protein environment.[1] The accuracy and applicability of the method will be illustrated by a recent work on Histone deacetylase.[2]\n\u003C\/p\u003E\n\u003Cp\u003ESecondly, I will emphasize ways to use the magnetic chemical shielding function to probe electron delocalization and design new electron delocalized systems. [4,5]\n\u003C\/p\u003E\n\u003Cp\u003EFinally, I will move toward the analysis of electron delocalization in biological systems by mentioning some future challenges. \n\u003C\/p\u003E\n\u003Cp\u003E[1] Zhang, Y.; Lee, T. S.; Yang, W. J. Chem. Phys. 1999, 110, 46.\u003Cbr \/\u003E\n[2] Corminboeuf, C.; Hu, P.; Tuckerman, M. E.; Zhang, Y. J. Am. Chem. Soc. ASAP.\u003Cbr \/\u003E\n[3] C. Corminboeuf, T. Heine, G. Seifert, P. v. R. Schleyer and J. Weber Phys. Chem. Chem. Phys. 2004, 6, 273.\u003Cbr \/\u003E\n[4] Heine, T. Corminboeuf, C.; Seifert, G. Chem. Rev. 2005, 105, 3889.\u003Cbr \/\u003E\n[5] Chen, Z. ; Wannere, C. S.; Corminboeuf, C.; Putcha, R.; Schleyer, P. v. R.; Chem. Rev. 2005, 105, 3842.\n\u003C\/p\u003E\n\u003Cp\u003EFor more information contact \u003Ca href=\u0022mailto:jean-luc.bredas@chemistry.gatech.edu\u0022\u003EDr. Jean-Luc Br\u00e9das\u003C\/a\u003E (404-385-4986).\n\u003C\/p\u003E","summary":null,"format":"limited_html"}],"field_subtitle":"","field_summary":[{"value":"Dr. Clemence Corminboeuf, Center for Computational Chemistry, University of Georgia","format":"limited_html"}],"field_summary_sentence":[{"value":"Dr. Clemence Corminboeuf,  Univ of Georgia"}],"uid":"27275","created_gmt":"2006-04-07 00:00:00","changed_gmt":"2016-10-08 01:57:36","author":"Shirley Tomes","boilerplate_text":"","field_publication":"","field_article_url":"","field_event_time":{"event_time_start":"2006-04-12T12:00:00-04:00","event_time_end":"2006-04-12T13:00:00-04:00","event_time_end_last":"2006-04-12T13:00:00-04:00","gmt_time_start":"2006-04-12 16:00:00","gmt_time_end":"2006-04-12 17:00:00","gmt_time_end_last":"2006-04-12 17:00:00","rrule":null,"timezone":"America\/New_York"},"extras":[],"groups":[{"id":"85951","name":"School of Chemistry and Biochemistry"}],"categories":[],"keywords":[{"id":"960","name":"physics"}],"core_research_areas":[],"news_room_topics":[],"event_categories":[{"id":"1795","name":"Seminar\/Lecture\/Colloquium"}],"invited_audience":[],"affiliations":[],"classification":[],"areas_of_expertise":[],"news_and_recent_appearances":[],"phone":[],"contact":[{"value":"\u003Cstrong\u003EShirley Tomes\u003C\/strong\u003E\u003Cbr \/\u003EChemistry \u0026amp; Biochemistry\u003Cbr \/\u003E\u003Ca href=\u0022http:\/\/www.gatech.edu\/contact\/index.html?id=st81\u0022\u003EContact Shirley Tomes\u003C\/a\u003E\u003Cbr \/\u003E\u003Cstrong\u003E404-894-0591\u003C\/strong\u003E","format":"limited_html"}],"email":[],"slides":[],"orientation":[],"userdata":""}}}