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. 2017 Sep 11;114(39):E8194–E8203. doi: 10.1073/pnas.1706197114

Table S1.

Rotational and translational diffusion of Ddx4

Protein Concentration MW(kDa) D(cm2/s)* RH <S2τc> (ns)
Ubiquitin§ 8.5 2.0 × 10−6 (±0.1) 15.7 3.3
Ddx4dil 7 mg/mL 25.8 8.8 × 10−7 (±0.2) 31.6 1.5(±0.5)
Ddx414FtoA D0# 24.8 9.0 × 10−7 (±0.1) 30.9
Ddx414FtoA 250 mg/mL 24.8 3.5 × 10−8 (±0.1) ** 2.4(±0.8)
Ddx414FtoA 370 mg/mL 24.8 9.2 × 10−9 (±0.9) ** 4.8(±1.5)
Ddx4cond 380 mg/mL 25.8 7.5 × 10−9 (±0.4) ** 8.5(±3)
Ddx4cond†† 440 mg/mL 25.8 5.4 × 10−9 (±0.4) ** 10.4(±4)

D0, concentration extrapolated to 0; MW, molecular mass.

*

Measured by pulsed field gradient NMR as described in SI Materials and Methods (30 °C).

Hydrodynamic radius (RH) calculated from measured diffusion coefficient in buffer along with diffusion of acetate (30 °C) (SI Materials and Methods).

Product of square of order parameter for backbone amide, S2, and residue-specific overall tumbling time, τC, averaged over residues for which data is available (30 °C).

§

<S2τc> data from refs. 57 and 58.

Sample obtained from the dilute phase of phase-separated Ddx4

#

Extrapolated from self-diffusion data as a function of concentration to zero concentration.

Relaxation data not measured.

**

Hydrodynamic radius cannot be accurately extracted from diffusion measurements on concentrated samples because of elevated viscosity. All estimates of RH make use of dilute Ddx4 samples.

††

A lower NaCl concentration was used (7.5 mM) relative to all other Ddx4 samples to achieve a higher protein concentration in the condensed phase.