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. Author manuscript; available in PMC: 2014 Dec 10.
Published in final edited form as: Biochemistry. 2013 Nov 22;52(49):8907–8915. doi: 10.1021/bi401494f

Table 1.

Properties of Y, 3,5-F2Y, α3Y and α3(3,5)F2Y

System λmax (nm) / ε (M–1 cm–1) pKa [pKapp] Potential vs. NHE (mV)e Ref.
Y(Ac/NH2)a 275/1400 (Y-OH)
293/2420 (Y-O-)
10 Epeak 830 (pH 7.0) 31
3,5-F2Y(Ac/NH2)a 263/560 (Y-OH)
275/1830 (Y-O-)
7.0 ± 0.2 Epeak 770 (pH 7.0) 31
α3Y 277/1500 (Y-OH, pH 5.4)
294/2430 (Y-O-, pH 13.4)
[11.3 ± 0.1] E°' 1059 (pH 5.7)
E°' 980 (pH 7.0)
10, 22, 23 this work
α3(3,5)F2Y ~264/n.d. (Y-OH)a
~277/n.d. (Y-O-)a
[8.0 ± 0.1] E°' 1026 (pH 5.7)
E°' 952 (pH 7.0)f
this work
System [Θ]222 × 103 (deg cm2 dmol–1) Helix (%)b ΔG (kcal mol–1)g Ref.
α3Y −20.0 ± 0.8 (pH 5.6) 75 ± 3 (pH 5.6)c
74 ± 1 (4.5-10)d
−3.7 ± 0.1 (pH 5.0)
−3.9 ± 0.1 (pH 5.5)
10, 22, this work
α3(3,5)F2Y −20.9 ± 0.6 (pH 5.6) 79 ± 2 (pH 5.6)c −3.7 ± 0.1 (pH 5.0)
−3.7 ± 0.1 (pH 5.5)
this work
a

Acetyl-tyrosinamide (Ac/NH2), ε was not determined (n.d.).

b

Scaled relative to the [Θ]222 of α3W (76 ± 1% α-helical, pH 4-10; 10, 25).

c

[Protein] determined by the Bradford assay.

d

[Protein] determined by UV absorption (10, 22).

e

Anodic peak potentials from irreversible differential pulse voltammograms (Epeak; 10, 11, 31). The standard error in E°' is ± ± 4 mV.

f

Extrapolated from the pH 5.7 value and assuming the same pH dependence as observed for α3Y '(pH 5.7) and E°'(pH 7.0)(23).

g

From Fig. S5.