Hey Shahab, What's the contradiction?
> [ Furthermore, INT–DBD appears less compact in the complex, as far as the > radius of gyration increases and more molecular surface is exposed to the > solvent (Table 1). ] larger radius of gyration, less compact, more surface > [ Furthermore, according to radiuses of gyration of two proteins in the two > systems, the protein in the complex is more > compact than the free protein, this is consistent with the result of > structure stability comparing. It means that less > molecular surface of homeodomain protein in the protein– DNA complex is > exposed to the solvent.] (smaller radius of gyration; not stated explicitly), more compact, less surface. Seems consistent to me... Cheers, Tsjerk -- Tsjerk A. Wassenaar, Ph.D. post-doctoral researcher Molecular Dynamics Group * Groningen Institute for Biomolecular Research and Biotechnology * Zernike Institute for Advanced Materials University of Groningen The Netherlands -- gmx-users mailing list gmx-users@gromacs.org http://lists.gromacs.org/mailman/listinfo/gmx-users Please search the archive at http://www.gromacs.org/Support/Mailing_Lists/Search before posting! Please don't post (un)subscribe requests to the list. Use the www interface or send it to gmx-users-requ...@gromacs.org. Can't post? Read http://www.gromacs.org/Support/Mailing_Lists
