SAXS, if the motion is not random and especially if you have crystallographic/NMR structure for the domains.. Edward Snell Ph.D. Assistant Prof. Department of Structural Biology, SUNY Buffalo, Senior Scientist, Hauptman-Woodward Medical Research Institute 700 Ellicott Street, Buffalo, NY 14203-1102 Phone: (716) 898 8631 Fax: (716) 898 8660 Skype: eddie.snell Email: esn...@hwi.buffalo.edu Telepathy: 42.2 GHz
Heisenberg was probably here! From: CCP4 bulletin board [mailto:ccp...@jiscmail.ac.uk] On Behalf Of Daniel Jin Sent: Monday, December 06, 2010 11:59 AM To: CCP4BB@JISCMAIL.AC.UK Subject: [ccp4bb] pH dependent conformational change Dear CCP4 colleagues, We have a protein that is composed of two domains connected by a short peptide linker. We have some indirect evidence showing that the two domains may somehow move against each other when exposed to different pH. It is unlikely to have any obvious secondary structure change since each domain behaves like a rigid body. I am wondering whether there is any “easy” way, biochemically or biophysically, to monitor the conformational changes in solution. Many thanks. As far as I know most of the pH sensing stories are linked to histidine residue. Can you point me to any references that show a different pH sensing mechanism (other than His)? Thanks. Best, Daniel
