Abstract
It has been suggested that in ‘dry’ protein-trehalose-water systems, water-mediated hydrogen bond network, whose strength increases by drying, anchors the protein to its surroundings. To further characterize this effect, we performed a DSC study on low-water myoglobin-trehalose systems. The denaturation temperature resulted to increase by decreasing hydration, and linearly correlated to the glass transition temperature of both the ternary protein-water-trehalose and the binary water-trehalose systems. Further measurements are being performed to investigate eventual differences among different saccharides.
Sign-in/Register to access full text options 
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.
