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| Tuesday, March 1, 2011
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12:30 PM - 1:30 PM
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3:00 PM - 4:00 PM
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4:00 PM - 5:00 PM
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| Wednesday, March 2, 2011
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11:30 AM - 1:00 PM
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Bioinformatics Seminar Series:Ensemble Predictions of beta-sheet Protein Structures
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| Description: |
Speaker: Jerome Waldispuhl, McGill. TOC Lab Stata Center Room G575
In this talk, I will describe my work in the area of protein structure prediction. I will introduce new ensemble modeling techniques which can analyze and predict an entire landscape of structural solutions, rather than simple single answer optimizations. This philosophy has a broad impact on our understanding of protein folding properties.
To describe our methods, I will start by illustrating how these techniques have been applied to transmembrane beta-barrel proteins. I will introduce a new family of algorithms for investigating this family proteins based only on sequence information, broad investigator knowledge, and a statistical-mechanical approach using the Boltzmann partition function. This provides predictions
of all possible structural conformations that might arise in-vivo, along with their relative likelihood of occurrence. Using a parameterizable grammatical model, these algorithms incorporate high-level information, such as membrane thickness, with an energy function based on stacked amino-acid pair statistical potentials to predict ensemble properties, such as the likelihood of
two residues pairing in a beta-sheet, or the per-residue X-ray crystal structure B-value.
In the second part of this talk, I will show how to generalize our methods for modeling ensembles of generic beta-sheet structures. From this ability to compute a realistic representation of the conformational landscape, we build a coarse-grained model of the energy landscape which is used to simulate folding processes. We illustrate our methods for dynamics prediction by applying it to
the folding pathway of the well-studied Protein G. With relatively very little computation time, we show that our program tFolder is able to reveal critical features of the folding pathways which were only previously observed through time-consuming molecular dynamics simulations and experimental studies.
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| Contact: |
Patrice Macaluso
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2:00 PM - 3:20 PM
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Amyotrophic Lateral Sclerosis: Lessons from Genetics
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| Description: |
Robert Brown, M.D., Chairman of Neurology, University of Massachusetts Medical Center, Worcester, MA. Boston University School of Medicine, 72 East Concord Street, L-112, Boston, MA. Part of the Current Topics in Pharmacological Sciences Seminar Series sponsored by the Department of Pharmacology & Experimental Therapeutics. Free and open to the public. Refreshments served at 1:45 pm, R-Building 6th Floor.
www.bumc.bu.edu/busm-pm
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| Contact: |
Kristina Bigdeli
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4:00 PM - 5:00 PM
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Neuroscience Seminar - Peter Kalivas
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| Description: |
Tufts University Neuroscience Seminar
Peter Kalivas, PhD
Medical University of South Carolina
Title: "New treatments for addiction hiding in synaptic plasticity"
Location:
150 Harrison Avenue, Jaharis 508
Boston, MA
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| Contact: |
Laila Lee
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| Thursday, March 3, 2011
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Noon - 1:00 PM
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Translational Control of the Heme-Regulated eIF2a Kinase in Oxidative Stress and Erythropoiesis
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| Description: |
Location: The Forsyth Institute, Seminar Room A
245 First Street, 17th Floor
Cambridge
Speaker: Jane-Jane Chen, PhD
Principal Research Scientist
Harvard-MIT Division of Health Sciences and
Technology, MIT
Abstract: Maturation of erythroid precursors requires active synthesis of a very large amount (350 mg/ml) of hemoglobin, which consists of two pairs of ƒÑ- and ƒÒ-globin subunits with each monomer bound to a heme moiety. Excess of any of these three components of hemoglobin is cytotoxic. Heme-regulated eIF2ƒÑƒnkinase (HRI) balances synthesis of heme and globin by sensing the intracellular heme concentration. In heme deficiency, HRI is activated and phosphorylates the ƒÑ-subunit of eukaryotic initiation factor (eIF2ƒÑ), which impairs the recycling of eIF2 for translational initiation and results in cessation of protein synthesis. Beyond heme deficiency, HRI is also the predominant eIF2ƒÑ kinase activated by arsenite-induced oxidative stress, heat shock and UV irradiation in erythroid cells. Thus, HRI may protect erythroid cells against stress generally and may play a role in the physiological response to intrinsic disorders of red blood cells. Indeed, HRI deficiency in mice exacerbates erythropoietic protoporphyria and renders ƒÒ-thalassemia embryonically lethal. In addition to general inhibition of protein synthesis, phosphorylation of eIF2ƒÑ by HRI also leads to a selective increased translation of ATF4 mRNA in erythroid precursors and the subsequent induction of gene transcription for the adaptation to acute oxidative stress and chronic iron deficiency. Hri-/- mice develop ineffective erythropoiesis in iron deficiency with an inhibition of erythroid differentiation at the basophilic stage. Together, these results underscore a functional role of HRI signaling pathways in stress erythropoiesis to mitigate the stress arisen from both erythroid milieu and intrinsic red cell disorders.
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| Contact: |
Pam Quattrocchi
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4:00 PM - 5:00 PM
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4:30 PM - 5:30 PM
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Vascular Biology Seminar: Dipak Panigrahy, MD
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| Description: |
Dipak Panigrahy, MD
Instructor in Surgery, Harvard Medical School
Vascular Biology Program, Children's Hospital Boston
“The Role of Epoxyeicosatrienoic Acids in Cancer Metastasis and Regeneration: The Folkman Legacy Revisited”
4:30 PM
Folkman Auditorium, Enders Bldg
Children's Hospital Boston, 320 Longwood Ave.
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| Contact: |
David Lynn, 617-525-4351
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| Friday, March 4, 2011
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8:30 AM - 9:30 AM
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1:30 PM - 2:45 PM
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Week of Sunday, February 27, 2011
