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Dear All, I would like to compare the flexibility of the secondary structure elements forming the active site in homologous proteins. What are the possible methods of doing it? Not all the homologs have high sequence similarity (<50% similarity). I have looked at some older threads on the BB regarding usage of B-factors. While some have suggested the addition of a constant to the model with the lower B-factors to compare to the one with other B-factors, others have commented that it is not valid to compare B-factors for data collected from different crystals. Also, B-factor based-analysis can't be carried out when the homologs have NMR structures. Any suggestions? The tools may also include software/servers outside the CCP4 suite . Looking forward to your replies, Thanks and regards,Ms. Sreetama Das PhD student,Dept. of Physics,Indian Institute of Science