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. 2020 Apr 18;118(10):2470–2488. doi: 10.1016/j.bpj.2020.04.010

Table 1.

Mass and Size of the Different Phosphoprotein Constructs

Protein Naaa pIcalcb MMcalc (kDa)c MMexp (kDa)d Rh,folded (nm)e Rh,unfolded (nm)e Rh,exp (nm)f Rg,theo(Bernado) (nm)g Rg,theo(Fitskee) (nm)h Rg,exp nm)i Dmax (nm)j
P1–100 108 5.1 12.347 13.5 ± 1.5 1.8 3.1 2.6 ± 0.2 2.9 3.4 3.2 ± 0.1 12
P92–190 108 4.9 11.875 12.0 ± 0.5 1.8 3.0 2.6 ± 0.2 2.9 3.4 3.1 ± 0.2 12
P173–240 78 6.4 8.691 8.0 ± 2 n.d. n.d. n.d. n.d. n.d. n.d. n.d.
P92–250 168 4.6 18.583 21.0 ± 2.0 n.d. n.d. n.d. 3.7 4.5 4.0 ± 0.3 15
P223–319 106 4.5 11.536 12.9 ± 1.5 1.8 3.0 3.1 ± 0.2 2.9 3.4 3.1 ± 0.1 11.5
P300–401 111 5.9 12.421 11.5 ± 1.5 n.d. n.d. n.d. 2.9 3.5 n.d. n.d.
P387–479 102 7.1 11.151 12.4 ± 1.5 1.8 3.0 2.5 ± 0.2 3.3 3.3 3.2 ± 0.1 12.5
P471–580∗ 119 5.2 13.757 (55.028) 58 ± 6 3.1 6.7 4.3 ± 0.2 n.r. n.r. n.d. n.d.
P655–709 63 5.3 7.364 8 ± 1 n.d. n.d. n.d. 2.2 2.5 1.6 ± 0.1 5.5
P588–650 72 5.3 8.289 8 ± 2 n.d. n.d. n.d. 2.4 2.7 2.6 ± 0.1 10
P588–709 131 4.9 15.041 15.3 ± 1 1.6 2.5 1.9 ± 0.2 n.d. n.d. n.d. n.d.
P1–580∗ 588 4.7 64.756 (259.024) 250 ± 25 5.5 14.8 9.2 ± 0.3 n.r. n.r. 10.8 ± 0.3 41
P471–709∗ 248 4.9 28.369 (113.476) 113 ± 10 4.1 9.8 7.8 ± 0.3 n.r. n.r. 6.3 ± 0.1 22
PFL∗ 717 4.7 79.367 (317.468) 306 ± 30 6.0 16.8 9.3 ± 0.2 n.r. n.r. 10.9 ± 0.1 39

n.d., not determined; n.r., not relevant.

∗

Proteins that were found to be tetrameric in solution.

a

Number of amino acids in the used constructs, including C-terminal His tag and linker (LEHHHHHH) and, in some cases, an N-terminal M.

b

Isoelectric point of the used constructs calculated using the webserver ProtParam. In parentheses, isoelectric point calculated without the C-terminal His tag.

c

In parentheses, calculated mass for a tetramer.

d

Measured by SEC-MALLS.

e

The theoretical Rh-values are calculated from Rh-values of folded and chemically unfolded standard proteins taken from Uversky et al. (56) and using the experimental molecular mass determined by SEC-MALLS.

f

Measured from SEC data by calibrating the system with standard globular proteins.

g

Calculated using the power law and parameters defined by Bernado et al. (88)

h

Calculated using the power law and parameters defined by Fitskee et al (87).

i

Measured from SAXS data at low Q using the Guinier approximation.

j

Determined from SAXS data using the program PRIMUS.