A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro -- Data Supplement - Supplemental Data -- Proceedings of the National Academy of Sciences

Supplementary material for Ramírez-Alvarado et al., Proc. Natl. Acad. Sci. USA, 10.1073/pnas.150091797

Table 2.
Expected fibril formation based on the unfolding transition range from thermal denaturation curves

Protein	Unfolding transition range	pH 5.2 338 K	Unfolding transition range pH 9.02	pH 9.02 313 K	pH 9.02 333 K	pH 9.02 353 K	Unfolding transition range pH 9.02 1 M Na₂SO₄	pH 9.02 313 K 1 M Na₂SO₄	pH 9.02 333 K 1 M Na₂SO₄	pH 9.02 353 K 1 M Na₂SO₄
WT	343 K -	-	333 K-353 K	-	-	-	338 K-363 K	-	-	+
I6T53	338-363 K	-	313 K-347 K	+	+	-	333 K-359 K	-	-	+
A6Y53	313-363 K	+	293 K-330 K	-	-	-	309 K-355 K	+	+	+
A6F53	313-363 K	+	293 K-337 K	+	+	-	313 K-353 K	-	+	+
F6A53	313-343 K	+	303 K-333 K	+	-	-	308 K-355 K	+	+	-
F6G53	298-343 K	+	283 K-323 K	+	-	-	303 K-330 K	+	-	-
A6A53	298-339 K	+	285 K-327 K	+	-	-	298 K-333 K	+	-	-
G6Y53	298-340 K	+	277 K-319 K	+	-	-	293 K-333 K	+	+