Fwd: Special Seminar

Karin Lustre karin at cs.uchicago.edu
Wed Jan 10 10:20:37 CST 2001


>X-Sender: mkulberg at nsit-imap.uchicago.edu (Unverified)
>Date: Wed, 10 Jan 2001 09:51:43 -0600
>To: eder at oddjob.uchicago.edu, karin at cs.uchicago.edu, marg at geosci.uchicago.edu,
>    kennedy at math.uchicago.edu, j-chernick at uchicago.edu,
>    gilpin at galton.uchicago.edu, bit1 at midway.uchicago.edu,
>    rg-garrison at uchicago.edu
>From: Mary Kulberg <mkulberg at midway.uchicago.edu>
>Subject: Special Seminar
>
>Please distribute via your departmental/institute e-mail:
>
>The Department of Computer Science, Bioinformatics,
>and the Institute for Biophysical Dynamics (IBD) at
>The University of Chicago
>
>present a Special Seminar
>Monday, January 22, 2001 at 2:30 in CLSC 101
>Refreshments in CLSC 119 at 2:15
>
>Hybrid of Electron Cryo-Microscopy and Bioinformatics to Reveal Protein
>Folds in Domains of Biological Machines
>
>Wah Chiu, National Center for Macromolecular Imaging
>Professor of Biochemistry and Director of
>Graduate Program in Structural and Computational Biology and Molecular
>Biophysics, Baylor College of Medicine, Houston, Texas
>
>Abstract
>Few large biological machines have been solved to atomic resolution, 
>resulting in under-representation in the library of known structures 
>and folds. Thus, it is likely these large complexes might contain 
>many yet unidentified folds, providing an enriched source of novel 
>folds. However, it is often difficult to achieve a high-resolution 
>model for these structures. Electron cryo-microscopy is capable of 
>determining structures of large assemblies at low to intermediate 
>resolutions. To aid in the interpretation and analysis of such 
>structures, we have developed a computational method to identify 
>potential homologous folds based on the arrangement of alpha helix 
>elements, resulting in a structure-based recognition of folds 
>containing alpha helices. In addition, we can use sequence-based 
>threading to predict fold in a small domain of a large complex and 
>then fit the putative fold within a region of the target structure. 
>The structural fitting therefore provides a quantitative means to 
>further examine the architecture and organization of large, complex 
>machine. Applications of these methods to study large animal virus 
>such as herpesvirus capsid and skeletal muscle calcium release 
>channel will be demonstrated.
>http://bioinformatics.cs.uchicago.edu/
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