For information about this Alzheimer's lecture series, see: http://int.lanl.gov/news/index.php/fuseaction/nb.story/story_id/13644/nb_date/2008-06-19
---------------------------------------------------------------------------- Proteins behaving badly: Link between misfolding and Alzheimer's disease Gnana Gnanakaran Research Talk Background: Proteins need to adopt three-dimensional shapes (native fold) to function properly. Information needed to adopt the native fold is encoded in the chain of aminoacids that are easily obtained from genome sequencing projects. However, the protein folding problem, how a linear chain of amino acids attains the functional shape, still remains a challenging research activity. When a protein misfolds, cellular mechanisms are in place to detect and degrade it before it can become toxic. Despite these efforts, a range of debilitating human diseases is associated with protein misfolding. Lately, most attention has been paid to a group of diseases where proteins or peptides convert from their normally soluble forms to aggregates of insoluble fibrils or plaques. The final forms of these aggregates often have an ordered assembly of cross¾-sheet fibrils and referred as amyloids. The deposits of amyloid are associated with at least 20 diseases, including such diverse entities as Alzheimer's disease, prion disease, type 2 diabetes mellitus, Parkinson's disease and Huntington's disease. In this talk we will present results from all-atom computer simulations that considered the monomer and oligomers of the aggregation-prone fragment of amyloid beta peptide which is implicated in the Alzheimer's disease. These simulations are motivated by the clinical studies that have suggested oligomers as the possible pathological agents. We provide a thorough understanding of oligomer formation with detailed picture of forces that drive the interaction between fragments. Collaborative research with Ruth Nussinov (National Cancer Institute) and Angel Garcia (RPI). Calculations were carried out on PINK as part of the institutional computing project at LANL. Funded by LANL/DOE LDRD program ============================================================ FRIAM Applied Complexity Group listserv Meets Fridays 9a-11:30 at cafe at St. John's College lectures, archives, unsubscribe, maps at http://www.friam.org
