Journal article
The role of protein stability, solubility, and net charge in amyloid fibril formation
Protein science, Vol.12(10), pp.2374-2378
10/2003
DOI: 10.1110/ps.03152903
PMCID: PMC2366926
PMID: 14500896
Abstract
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.
Details
- Title: Subtitle
- The role of protein stability, solubility, and net charge in amyloid fibril formation
- Creators
- Jason P. Schmittschmitt - Texas A&M UniversityJ. Martin Scholtz - Texas A&M University
- Resource Type
- Journal article
- Publication Details
- Protein science, Vol.12(10), pp.2374-2378
- DOI
- 10.1110/ps.03152903
- PMID
- 14500896
- PMCID
- PMC2366926
- NLM abbreviation
- Protein Sci
- ISSN
- 0961-8368
- eISSN
- 1469-896X
- Language
- English
- Date published
- 10/2003
- Academic Unit
- Research Administration; Pharmaceutical Sciences and Experimental Therapeutics; Biochemistry and Molecular Biology; Chemistry
- Record Identifier
- 9984293088702771
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