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. 2004 Sep 17;87(6):3982–3994. doi: 10.1529/biophysj.104.048454

TABLE 3.

Results of fits to 17O and 2H MRD data from SNase mutants at 20°C

From 17O MRD data
From 2H MRD data
SNase variant pH CP (mM)* Inline graphic Inline graphic Inline graphic Inline graphic Inline graphic Inline graphic
Δ+PHS 4.5 1.59 2.0 ± 0.1 1.45 ± 0.04 3.8 ± 0.3 1.5 ± 0.3 3.2 ± 0.1 4.8 ± 0.8
Δ+PHS 7.0 1.59 2.3 ± 0.2 1.70 ± 0.06 5.0 ± 0.4 2.1 ± 0.2 2.2 ± 0.1 4.6 ± 0.4
Δ+PHS 9.5 1.59 2.5 ± 0.2 1.73 ± 0.06 4.3 ± 0.4 1.9 ± 0.5 4.8 ± 0.2 12 ± 2
Δ+PHS/V66K 4.5 0.85 1.7 ± 0.2 1.64 ± 0.06 3.3 ± 0.5 1.4 ± 0.4 3.4 ± 0.2 3.9 ± 1.0
Δ+PHS/V66K 7.0 1.44 2.4 ± 0.2 1.76 ± 0.06 4.0 ± 0.5 2.1 ± 0.2 2.1 ± 0.1 4.3 ± 0.6
Δ+PHS/V66E 7.0 1.18 2.3 ± 0.2 1.81 ± 0.06 4.5 ± 0.4 2.2 ± 0.3 2.1 ± 0.1 4.5 ± 0.9
Δ+PHS/V66E 9.5 1.00 2.1 ± 0.2 1.81 ± 0.07 4.6 ± 0.5 1.5 ± 0.5 4.8 ± 0.2 14 ± 2

All MRD profiles were subjected to bi-Lorentzian fits with three adjustable parameters and the two correlation times were fixed at the mean values, τβ = 12.6 ns and τγ = 2.1 ns, obtained from unconstrained fits.

*

Protein concentration in MRD sample.