<font size="2"><span style="font-family: times new roman,serif;">Dear Tsjerk</span><br style="font-family: times new roman,serif;">
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<span style="font-family: times new roman,serif;">thanks for your reply.</span><br style="font-family: times new roman,serif;">
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<span style="font-family: times new roman,serif;">in paper 1 :</span><br style="font-family: times new roman,serif;">
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<pre style="font-family: times new roman,serif;"><font size="2">larger radius of gyration, less compact, more surface<br><br>in paper 2: <br>(smaller radius of gyration; not stated explicitly), more compact, less surface.<br>
<br>in paper 3:<br><br>[Journal of Structural Biology 156 (2006) 537–545]<br><br>Overall, the GBD appears a little more compact in the complex, as far as the radius<br>of gyration decrease and less molecular surface is exposed to the solvent.<br>
<br>all of above is true.<br><br>I want to know exactly how do radius of gyration of protein from free state to complex state change .<br>Rg increased od decreased?<br><br></font>What's the contradiction?<br><br>contradiction is in this that in paper 1 Rg increased and in paper 2 and 3 decreased.<br>
<br>I want to know my data [ In my simulation systems, the average of radius of gyration in free protein<br>is 2.31 and for protein in complex is 2.58.] is true?<br></pre>