BIOT 231 |
| Replacement of one amino acid for another within a protein sequence alters a number of physicochemical properties at one time (e.g., size, hydrophobicity, polarity). Therefore, a multivariate approach to analyzing the effects of mutation on aggregation propensity must be taken. We have used reduced properties of amino acids and used them to analyze protein sequences, in an effort not only to identity the critical residues, but also the specific physicochemical property at that site having the greatest impact on aggregation rate. The application of this approach to antibody light chains will be presented, along with results on A-beta peptide mutants. In addition, the methodology has been used to study the sequence dependence of conformational stability of the variable region of antibody light chains, as increased conformational stability is critical for retarding aggregation. |
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Biophysical and Biomolecular Symposium: Protein Aggregation
3:00 PM-5:20 PM, Wednesday, August 22, 2007 BCEC -- 108, Oral
Division of Biochemical Technology |