{"120351":{"#nid":"120351","#data":{"type":"event","title":"Prof. John Straub, Boston University","body":[{"value":"\u003Cp\u003EProf. John Straub, Boston University\u003C\/p\u003E\u003Cp\u003E\u003Cem\u003E\u003Cstrong\u003ERole of Sequence and Membrane on Amyloid Precursor Protein Structure and Function\u003C\/strong\u003E\u003C\/em\u003E\u003C\/p\u003E\u003Cp\u003ESchool Colloquia\u003C\/p\u003E\u003Cp\u003EAggregation of proteins of known sequence is linked to a variety of neurodegenerative disorders. The amyloid \u03b2 (A\u03b2) protein associated with Alzheimer\u0027s Disease (AD) is derived from cleavage of the 99 amino acid C-terminal fragment of Amyloid Precursor Protein (APP-C99) by \u03b3-secretase. Certain familial mutations of APP-C99 have been shown to lead to altered production of A\u03b2 protein and the early onset of AD. We describe simulation studies exploring the structure of APP-C99 in micelle and membrane environments. Our studies explore how changes in sequence and membrane composition (including the presence of cholesterol) influence (1) the structure of monomeric APP-C99 and (2) APP-C99 homodimer structure and stability. Comparison of simulation results with recent NMR studies of APP-C99 monomers and dimers in micelle and bicelle environments provide insight into how critical aspects of APP-C99 structure and dimerization correlate with secretase processing, an essential component of the A\u03b2 protein aggregation pathway and AD.\u003C\/p\u003E\u003Cp\u003EFor more information contact Prof. Rigoberto Hernandez (404-894-0594).\u003C\/p\u003E\u003Cp\u003EWebsite: \u003Ca href=\u0022http:\/\/www.bu.edu\/chemistry\/faculty\/straub\/\u0022\u003EJohn Straub\u003C\/a\u003E\u003C\/p\u003E","summary":null,"format":"limited_html"}],"field_subtitle":"","field_summary":[{"value":"\u003Cp\u003EProf. John Straub, Boston University\u003C\/p\u003E\u003Cp\u003E\u003Cem\u003E\u003Cstrong\u003ERole of Sequence and Membrane on Amyloid Precursor Protein Structure and Function\u003C\/strong\u003E\u003C\/em\u003E\u003C\/p\u003E\u003Cp\u003ESchool Colloquia\u003C\/p\u003E","format":"limited_html"}],"field_summary_sentence":"","uid":"27275","created_gmt":"2012-03-29 08:32:21","changed_gmt":"2016-10-08 01:58:33","author":"Shirley Tomes","boilerplate_text":"","field_publication":"","field_article_url":"","field_event_time":{"event_time_start":"2013-02-28T20:00:00-05:00","event_time_end":"2013-02-28T21:00:00-05:00","event_time_end_last":"2013-02-28T21:00:00-05:00","gmt_time_start":"2013-03-01 01:00:00","gmt_time_end":"2013-03-01 02:00:00","gmt_time_end_last":"2013-03-01 02:00:00","rrule":null,"timezone":"America\/New_York"},"extras":[],"groups":[{"id":"85951","name":"School of Chemistry and Biochemistry"}],"categories":[],"keywords":[],"core_research_areas":[],"news_room_topics":[],"event_categories":[],"invited_audience":[],"affiliations":[],"classification":[],"areas_of_expertise":[],"news_and_recent_appearances":[],"phone":[],"contact":[{"value":"\u003Cp\u003EShirley Tomes (404-894-0591) \u003Ca href=\u0022mailto:shirley.tomes@chemistry.gatech.edu\u0022\u003Eshirley.tomes@chemistry.gatech.edu\u003C\/a\u003E\u003C\/p\u003E","format":"limited_html"}],"email":[],"slides":[],"orientation":[],"userdata":""}}}