Biophysical characterization of protein folding and misfolding.
Ribonuclease Sa and two charge-reversal variants can be converted into amyloidin 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 ivwell-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.
Advisor:Scholtz, J. Martin; LiWang, Andy C.; Pace, C. Nick; Kunkel, Gary
School:Texas A&M University
School Location:USA - Texas
Source Type:Master's Thesis
Keywords:protien folding stabilty
Date of Publication:12/01/2003