期刊
PROTEIN SCIENCE
卷 12, 期 10, 页码 2374-2378出版社
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1110/ps.03152903
关键词
amyloid; amyloid fibrils; pI; protein solubility; protein stability
资金
- NIGMS NIH HHS [GM52483, R29 GM052483, R01 GM052483] Funding Source: Medline
Ribonuclease Sa and two charge-reversal variants can be converted into amyloid in vitro by the addition of 2,2,2-triflouroethanol (TFE). We report here amyloid fibril formation for these proteins as a function of pH. The pH at maximal fibril formation correlates with the pH dependence of protein solubility, but not with stability, for these variants. Additionally, we show that the pH at maximal fibril formation for a number of well-characterized proteins is near the pI, where the protein is expected to be the least soluble. This suggests that protein solubility is an important determinant of fibril formation.
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