{"56217":{"#nid":"56217","#data":{"type":"event","title":"ChBE Spring2007 Seminar Series","body":[{"value":"\u003Cp\u003ECarlos F. Lopez, a Post-doc in the Department of Chemistry and Biochemistry at the University of Texas, Austin, presents \u003Cem\u003EOn The Hydrophilic Role of Hydrophobic Groups and Their Contributions to Cold Protein Denaturation\u003C\/em\u003E as part of ChBE\u0027s spring seminar series.\n\u003C\/p\u003E\n\u003Cp\u003E* Refreshments will be served at 3:30 PM in the Lower Level 1 Gossage Atrium\u003Cbr \/\u003E\n* Lecture commences at 4:00 PM in L1255 in the Ford ES\u0026amp;T Building\n\u003C\/p\u003E\n\u003Cp\u003ESeminar Abstract\u003Cbr \/\u003E\nProteins undergo structural transitions to denatured states when thermodynamic or chemical\u003Cbr \/\u003E\nperturbations are introduced to their native environment. Cold denaturation is an interesting\u003Cbr \/\u003E\nsolvent-driven phenomenon whereby proteins lose their hydrophobic associations leading to a\u003Cbr \/\u003E\ndenatured state. The currently accepted explanation for cold denaturation is tightly linked to a\u003Cbr \/\u003E\nfavourable change in the water to non-polar group interaction at cold temperatures which is\u003Cbr \/\u003E\nthought to eventually disrupt the protein tertiary structure. In this work we show how this\u003Cbr \/\u003E\nenvironmental perturbation leads to kinetic changes in the protein core due to a shift in the water\u003Cbr \/\u003E\nto non-polar atom interactions in apomyoglobin (apoMB). Analysis of our results shows that the\u003Cbr \/\u003E\nisothermal compressibility of the protein increases with decreasing temperature thus suggesting\u003Cbr \/\u003E\nan increase in the protein interstitial space. An increase in the number of solvent contacts around\u003Cbr \/\u003E\nthe protein, and in particular, around non-polar atoms suggests that the compressibility increase\u003Cbr \/\u003E\nis an indirect result of increased interfacial surface contacts. Atoms with increased\u003Cbr \/\u003E\ncompressibility and larger-than-expected fluctuations are localized within the protein core\u003Cbr \/\u003E\nregions. These results can be used to motivate an atomic level cold denaturation mechanism that\u003Cbr \/\u003E\nexplains and predicts protein structural changes under cold conditions. These results provide a\u003Cbr \/\u003E\nbasic biophysical explanation of the mechanism of denaturation away from ambient conditions\u003Cbr \/\u003E\nand how such conditions affect protein stability. As such, our results provide novel plausible\u003Cbr \/\u003E\npathways for the loss of protein structure, which could be important in fundamental biochemical\u003Cbr \/\u003E\nand biophysical processes, as well as subjects of medical nature such as diseases linked to\u003Cbr \/\u003E\nprotein structural transitions.\u003C\/p\u003E","summary":null,"format":"limited_html"}],"field_subtitle":"","field_summary":[{"value":"Carlos F. Lopez presents \u003Cem\u003EOn The Hydrophilic Role of Hydrophobic Groups and Their Contributions to Cold Protein Denaturation\u003C\/em\u003E as part of ChBE\u0027s spring seminar series.","format":"limited_html"}],"field_summary_sentence":[{"value":"Carlos F. Lopez presents seminar"}],"uid":"27255","created_gmt":"2010-05-20 11:47:16","changed_gmt":"2016-10-08 01:51:37","author":"Josie Giles","boilerplate_text":"","field_publication":"","field_article_url":"","field_event_time":{"event_time_start":"2007-02-07T15:00:00-05:00","event_time_end":"2007-02-07T16:00:00-05:00","event_time_end_last":"2007-02-07T16:00:00-05:00","gmt_time_start":"2007-02-07 20:00:00","gmt_time_end":"2007-02-07 21:00:00","gmt_time_end_last":"2007-02-07 21:00:00","rrule":null,"timezone":"America\/New_York"},"extras":[],"groups":[{"id":"1240","name":"School of Chemical and Biomolecular Engineering"}],"categories":[],"keywords":[{"id":"1303","name":"chbe"},{"id":"1704","name":"chemical \u0026 biomolecular engineering"},{"id":"2437","name":"lecture"},{"id":"166896","name":"seminar"}],"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\u003EJosie Giles\u003C\/strong\u003E\u003Cbr \/\u003ESchool of Chemical \u0026amp; Biomolecular Engineering\u003Cbr \/\u003E\u003Ca href=\u0022http:\/\/www.gatech.edu\/contact\/index.html?id=jg234\u0022\u003EContact Josie Giles\u003C\/a\u003E\u003Cbr \/\u003E\u003Cstrong\u003E404-385-2299\u003C\/strong\u003E","format":"limited_html"}],"email":[],"slides":[],"orientation":[],"userdata":""}}}