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. Author manuscript; available in PMC: 2009 Jan 25.
Published in final edited form as: J Mol Biol. 2007 Nov 13;375(4):1026–1039. doi: 10.1016/j.jmb.2007.11.014

Table 3.

Number of binding sites, n, and dissociation constants, KD, of T4L-L99A mutants binding to αB-D3 at 37°C (unless indicated), pH 7.2. The parameters were obtained from the non-linear least squares fit of binding curves consisting of at least 25 data points. F1 and F2 are the relative fluorescence of T4L bound in the high and low affinity modes, respectively. FU and FN are the fractional fluorescences in the unfolded and native states respectively. FN is normalized to 1. T4L concentration was fixed at 30 μM (unless indicated)

L99A Mutant n1 KD1 (μM) n2 KD2 (μM) F1 F2 ΔGTrp (FU/FN)bim
Q141Bi 0.2 0.02 0.54 0.57 2.38 0.97 5.1 0.42
Q141Bi/E22W 0.2 0.02 0.59 1.81 20.46 12.84 5.4 3.41
G113Bi 0.32 0.02 1.2 0.81 9.96 1.82 5.5 4.85
G113Bi/K83W † 0.2 0.05 1.08 0.74 21.7 8.49 4.9 5.59
N116Bi 0.28 0.01 0.99 0.35 1.25 0.69 5.1 0.54
N116Bi/N132W 0.2 0.08 0.65 6.3 39.5 30.7 6.3 9.94
V57Bi 0.22 0.01 1.0 2.04 1.0 0.78 5.0 1
V57Bi/K16W ‡ 0.34 0.29 1.2 30.01 17.32 14.79 4.8 12.09
L39Bi 0.35 0.11 1.2 11.65 2.79 1.67 4.9 2.19
L39Bi/Y25W 0.2 0.05 1.2 14.3 19.4 17.4 4.9 13.77
†

at 7.5 μM

‡

at 30°C

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