Dear all, Good morning, Sorry for the off-topic question.
There is a protein crystal sample in which water bonding networks by certain species to be studied by neutron diffraction, not exactly within the protein. But between the subunits of the protein. Now it is mandatory to use some D2O for the preparation of samples. Now my question is will there be drastic differences between the hydration patterns of this sample and original sample without D2O? For example, some change in positions and interacting partners of the hydrated species of interest with respect to the protein surface? Since deuterium has 2 electrons instead of one as in protium? We know D2O is regularly used for such experiments in Neutron diffraction and in NMR as well. Please let me know your expert opinions. Thank you. Best Regards, Arpita ######################################################################## To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB&A=1 This message was issued to members of www.jiscmail.ac.uk/CCP4BB, a mailing list hosted by www.jiscmail.ac.uk, terms & conditions are available at https://www.jiscmail.ac.uk/policyandsecurity/
