Figure 2 (IMAGE) Kanazawa University Caption Power law for relationship between radius gyration &lt;<i>R</i><sub>g</sub>&gt; and number of amino acids for 23 fully disordered regions: &lt;<i>R</i><sub>g</sub>&gt; = &beta;<sub>g</sub> &times; <i>N</i><sub>aa</sub><sup>&nu;</sup> (&beta;<sub>g</sub> = 0.26 nm, and &nu; = 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, &lt;<i>R</i><sub>2D</sub>&gt;, observed by HS-AFM was converted to &lt;<i>R</i><sub>g</sub>&gt; using &lt;<i>R</i><sub>g</sub>&gt; = <R2D>/(2&radic;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. Credit Kanazawa University Usage Restrictions The image may only be used with appropriate caption and credit. License Licensed content Disclaimer: AAAS and EurekAlert! are not responsible for the accuracy of news releases posted to EurekAlert! by contributing institutions or for the use of any information through the EurekAlert system.