BIOT 138 |
| Oxidation, deamidation and aggregation are common maladies affecting the integrity of protein molecules. Many biophysical and analytical tools are used commonly to empirically identify conditions that protect against degradation or contribute to it. The information generated from the standard methods has provided a basis for understanding the mechanisms by which these events occur. Nonetheless, increased resolution, in the form of residue-specific information, would further enable assessment and determination of how protein stabilization is accomplished. To address this issue, we developed a simple and rapid method in which heteronuclear, multidimensional solution NMR is applied to identify chemical and structural changes in proteins, which influence both its chemical and physical degradation. The effects of individual and combinations of excipients can be assessed quickly to determine which compounds promote protein stability. Combining the screening assay with addition NMR and/or other experiments generates mechanistic information to determine how stabilization is accomplished. |
|
Biophysical and Biomolecular Symposium: Protein Chemical Instability
8:00 AM-11:05 AM, Tuesday, August 21, 2007 BCEC -- 106, Oral
Division of Biochemical Technology |