CONFERENCE SPONSORS


CONFERENCE HOST UNIVERSITY AND GOLD SPONSOR:

Purdue University
Vice President, Office of Research
Bioinformatics Core


 SILVER SPONSORS:


Indiana University
University Information Technology Services
Department of Biology
School of Informatics and Computing
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University of Michigan, Dept of Computational Medicine and Bioinformatics

BRONZE SPONSORS:


The Research Division
of Ohio University
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Department of Computer Science and Engineering
Eck Institute for Global Health
Complex Networks Lab
University of Notre Dame


EXHIBITOR SHOWCASE SPONSOR:

 

Cincinnati Childrens’s Hospital Medical Center
Division of Biomedical Informatics, University of Cincinnati


POSTER AWARDS SPONSOR:


Faculty of 1000


BEST PAPER AWARD SPONSOR:


Springer


INDUSTRY SPONSOR:



University of Michigan Bioinformatics Core
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PerkinElmer


GENERAL SPONSOR:


Purdue University

Agricultural Research

Great Lakes Bioinformatics Conference 2015

PROMOTION


GLBIO 2015 Save the Date Flyer (.pdf)

 

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Image Credit:
Forbes Burkowski University of Waterloo, Canada  Insulin's Hydrophilic center

Forbes Burkowski
University of Waterloo, Canada

Insulin's Hydrophilic center
Usually one thinks of a protein as having a central hydrophobic core. In the case of insulin (PDB ID 1ZNJ) the structure is a “trimer of dimers”. Each of the trimers has a hydrophobic core but the entire structure surrounds a center that contains a hydrophilic “cage” structure containing two zinc atoms (one of which is seen in the image as a green sphere).

The image was created using VRML facilities in UCSF Chimera. Each of the residues is represented by a sphere that is given a color corresponding to the residue’s position in the Kyte-Doolittle hydrophobicity - hydrophilicity range. The corresponding color range is a linear interpolation going from orange to white to blue. Spheres having centers that are within a distance of 9 Angstroms are joined using a spindle.

For this image, all the spheres corresponding to hydrophobic residues were removed along with any incident spindles. The result reveals a compelling symmetric structure that arises from the original 3-fold symmetry of the protein.

Part of the ISMB ECCB 2013 Art and Science Exhibit
www.iscb.org/cms_addon/conferences/ismbeccb2013/artscience.php


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