Abstract
Antifreeze proteins (AFPs) are a class of ice-binding proteins that help cold-adapted organisms survive at subzero temperatures. Although the solution and crystal structures of many AFPs are known, solid-state NMR spectroscopy remains one of the few techniques with which their functional, ice-bound state can be studied at atomic resolution. This article describes solid-state NMR methods that investigate the protein–ice interaction of AFPs, methods that measure their remaining hydration shell, and methods that monitor the structural changes of AFPs on ice binding. Applications of these methods on type I and type III AFPs are presented. Keywords: frozen solution; protein hydration; protein binding; ice
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.
