ORGN 257 |
| Understanding the forces that control protein folding patterns remains a topic of widespread interest. Protein folding thermodynamics are generally studied via structure disruption with either heat or a chemical denaturant. Results obtained under partially denaturing conditions are extrapolated to native conditions in order to determine how changes in sequence are correlated with changes in stability. A concern with this approach is that the folded and unfolded states may differ between conditions under which the data are obtained and native conditions. We have developed a technique to study protein conformational stability under native conditions. A backbone amide group is replaced with a structurally analogous thioester group, and thiol-thioester exchange equilibria are then used to gain the desired information. Applications to small folding motifs will be discussed. |
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Frontiers in Bio-organic Chemistry and Chemical Biology
8:00 AM-11:55 AM, Monday, 14 March 2005 Convention Center -- Ballroom 20 C-D, Oral
Division of Organic Chemistry |