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PROBLEMS
P4.1. Calculation of Lifetimes: Use the data in Figures 4.1 and
4.2 to estimate the lifetime from the time-domain data,
and from the phase and modulation.
P4.2. Fractional Intensity of Components in the Tryptophan
Intensity Decay: At pH 7, tryptophan displays a doubleexponential
intensity decay. At 320 nm the intensity
decay low is I(t) = 0.19 exp(–t/0.62 ns) + 0.81
exp(–t/3.33 ns). What is the fractional contribution of
the 0.62-ns component to the steady-state intensity at
320 nm?
P4.3. Stacking Equilibrium in Flavin Adenine Dinucleotide:
Use the intensity decays and lifetimes in Figure 4.61 to
calculate the collisional rate between the flavin and adenine
groups in FAD.
P4.4. Average Lifetime: Suppose that a protein contains two
tryptophan residues with identical lifetimes (τ 1 = τ 2 = 5
ns) and pre-exponential factors (α 1 = α 2 = 0.5). Now
suppose that a quencher is added such that the first tryptophan
is quenched tenfold in both lifetime and steadystate
intensity. What is the intensity decay law in the
presence of quencher? What is the average lifetime (τ)
and the lifetime-weighted quantum yield ()? Explain
the relative values.
P4.5. Decay Associated Spectra: Tables 4.5 and 4.6 list the
results of the multi-exponential analysis of the two-component
mixture of anthranilic acid (AA) and 2-aminopurine
(2-AP). Use these data to construct the decay associated
spectra. Explain the results for the DAS recovered
from the non-global (Table 4.5) and global (Table 4.6)
analysis.