TABLE 1.
Protein | Barycentric mean wavelength (λm)a | Shifts in λmb | Ksvc |
---|---|---|---|
nm | nm | m−1 | |
b′x | 343.8 | 0.92 ± 0.05 (n = 3) | |
I272A b′x | 340.5 | −3.3 | 1.03 ± 0.02 (n = 2) |
L343A b′x | 349.6 | +5.8 | 2.14 ± 0.06 (n = 2)d |
W111F/W390F PDI | 348.7 | 0.84 ± 0.21 (n = 6) | |
W111F/W390F/I272A PDI | 346.8 | −1.9 | 0.92 ± 0.22 (n = 5) |
W111F/W390F/L343A PDI | 350.0 | +1.3 | 1.52 ± 0.17 (n = 4)d |
W111F abb′x | 345.6 | 0e | |
W111F/I272A abb′x | 342.9 | −2.7 | 0e |
W111F/L343A abb′x | 347.0 | +1.4 | 1.26 ± 0.05 (n = 3)d |
a The barycentric mean wavelength between 310 and 400 nm was calculated as λm = ΣF(λ)×(λ)/ΣF(λ), where F(λ) is the fluorescence intensity at wavelength λ (29).
b Difference of λm of I272A or L343A mutants minus λm of the corresponding background proteins. −, blue shift; +, red shift.
c Data were expressed as the mean ± S.D.
d p < 0.001.
e No quenching detectable.