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