This project was prepared as part of a BioQUEST faculty development workshop entitled Modeling in Bioinformatics at Lane Community College in October 2004. The BioQUEST Curriculum Consortium is committed to the reform of undergraduate biology instruction through an emphasis on engaging students in realistic scientific practices. This approach is sometimes characterized as an inquiry driven approach and is captured in BioQUEST's three P's (problem-posing, problem-solving, and peer-persuasion). As part of this workshop groups of faculty were encouraged to initiate innovative curricular projects. We are sharing these works in progress in the hope that they will stimulate further exploration, collaboration and development. Please see the following links for additional information:

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Structural Analysis of Amino Acid Sequence Variation of Immunoglobulin Epsilon Heavy Chain
 
 
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Authors


Lisa Sardinia
Pacific University


Jon Schnorr
Pacific University


Kurt Kreith
University of California, Davis

 
   
 


Possible Audiences:

peers  

 
 


Brief Overview:

Immunoglobulin protein (Ig), also known as antibody, is a major effector protein of the immune system. Produced by B cells, Ig has a highly conserved constant region and an antigen binding region that is hypervariable. Within this variable region, however, some amino acid sequences are more subject to variation than others. We examined this variation by constructing a sequence alignment of 9 human Ig epsilon heavy chain amino acid sequences. ConSurf was used to visualize the location of variable sites. Variation was not uniformly distributed; the greatest degree of variation was observed in the loops that extend to form part of the antigen binding site.  

 
   
 


Attachments


- Presentation1.ppt