Figure 2 (IMAGE)

Kanazawa University

Figure 2

Caption

Power law for relationship between radius gyration <<i>R</i><sub>g</sub>> and number of amino acids for 23 fully disordered regions: <<i>R</i><sub>g</sub>> = β<sub>g</sub> × <i>N</i><sub>aa</sub><sup>ν</sup> (β<sub>g</sub> = 0.26 nm, and ν = 0.52). The data plotted with the blue circles are those from the present SAXS study for four fully disordered segments of PQBP-1 (82-265, 82-214, 82-164, and 82-134). The nine data plotted with the cyan circles are from the present HS-AFM studies for different IDP constructs. The end-to-end distance of fully disordered regions, <<i>R</i><sub>2D</sub>>, observed by HS-AFM was converted to <<i>R</i><sub>g</sub>> using <<i>R</i><sub>g</sub>> = <R2D>/(2√3 <i>u</i>), where <i>u</i> = 1.24 was determined by best fitting of all 23 data to a power law, in which the parameter <i>u</i> was contained in the nine data as one of the variables to be determined. The 10 data plotted with the red circles are those from the SAXS study by Mylonas <i>et al</i>. for tau protein constructs [Biochemistry 47, 10345-10353 (2008)], with phosphor-mimic constructs and those significantly affected by the extended repeat domain having been removed here.

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Kanazawa University

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