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. 2013 Mar 7;8(3):e58297. doi: 10.1371/journal.pone.0058297

Table 3. Kinetic parameters for URN1-FF at pH 5.7.

Inline graphic 1(kcal mol−1) mU-F 2(kcal mol−1M−1) Cm 3 (M) kF (s−1) kU (s−1) RTmU(kcal mol−1 M−1) RTmF(kcal mol−1 M−1)
298 K 5.57±0.28 0.78±0.04 7.13±0.55 2741±95 0.23±0.11 0.19±0.04 0.59±0.01
310 K 5.28±0.04 0.81±0.04 6.50±0.34 7022±221 1.33±0.06 0.20±0.04 0.61±0.01
FBP114 3.64±0.05 1.16±0.02 3.14±0.07 2200±90 3.66±0.06 0.154±0.003 1.01±0.02
1

Gibbs energy of unfolding with urea determined from the kinetic parameters.

2

Dependence of the Gibbs energy of unfolding with urea.

3

The urea concentration required to unfold 50% of the protein molecules.

4

The values of the FF domain of HYPA/FBP11 were previously reported at 283 K [19].