Abstract
Protonation is the key to elucidate a function of protein.Neutron crystallographic analysis is a powerful method that can observe the protonation states of amino acid residues in a protein molecule. However the neutron crystallographic technique was very difficult method, because of low flux neutron source mainly. Recently, a neutron imaging plate and an elastically bent perfect Si monochromator enabled neutron experiment. As the result, neutron structural biology has been progressed greatly in these ten years. In this report, we explain the various biological reactions affected by the protonation state on protein molecules by our studies on neutron crystallographic analysis. Furthermore, we also introduce our recent study on the protonation of cubic insulin molecule.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
