. 2012 Jun 5;287(31):25975–25984. doi: 10.1074/jbc.M112.372136

TABLE 1.

Conformational stability and properties of HuPrP(90–231) mutants

N.D., not determined; N.A., not applicable.

HuPrP mutant	Tm^a	ΔTm^b	Loss of α-helix^c	Accessible non-polar surface area^d
	°C	°C	%
WT (129M)	65.6 ± 0.4	0	12	125.0
M129A	62.4 ± 0.5	−3.1	12	80.4
M129V	66.1 ± 0.4	0.6	9	127.1
M129L	65.8 ± 0.4	0.3	10	156.0
M129P	58.4 ± 0.6	−7.2	15	ND
M129W	61.5 ± 0.4	−4.1	21	177.2
M129E	61.2 ± 0.4	−4.4	15	57.0
M129K	66.2 ± 0.3	0.7	8	109.3
M129C	65.7 ± 0.4	0.1	30	47.4
HuPrP(121–231)129M	65.3 ± 0.2	−0.3	11	NA
H187R	53.2 ± 0.6	−12.3	27	NA
F198S	48.6 ± 0.3	−17.0	17	NA

^a Midpoint of thermal denaturation measured by far UV circular dichroism at 222 nm.

^b Difference in midpoint of thermal denaturation in comparison with WT (129M).

^c Based on change in mean residue ellipticity measured by far UV circular dichroism at 222 nm before and after one round of thermal denaturation at 4–90 °C.

^d Data referring to the substituted amino acid obtained from Koh et al. (59), which calculated water-accessible non-polar surface areas (Å²) of the side chains in the fully extended β-form of the peptide Gly-X-Gly by using the Richmond algorithm (60) and van der Waals radii of Richards (61).