Backbone Thioester Exchange: A New Approach to Evaluating Higher Order Structural Stability in Polypeptides
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- 作者：Matthew G. Woll and Samuel H. Gellman
- 刊名：Journal of the American Chemical Society
- 出版年：2004
- 出版时间：September 15, 2004
- 年：2004
- 卷：126
- 期：36
- 页码：11172 - 11174
- 全文大小：100K
- 年卷期：v.126,no.36(September 15, 2004)
- ISSN：1520-5126
文摘
An amide bond has been replaced by a thioester in bovine pancreatic polypeptide (bPP) to allow rapid and reversible (dynamic) exchange of the 
ges/gifchars/alpha.gif" BORDER=0>-helical segment with other thiols in solution. We have begun to study the higher order structural stability of bPP by measuring the equilibrium constant of the "backbone thioester exchange" (BTE) reaction. The extent to which the equilibrium (KBTE) favors one set of peptides over the other, which can be easily measured, can be directly correlated to the energy gained from favorable noncovalent interactions that occur between peptide segments on either side of the thioester bond (Kfold).