Abstract
The transfer free energy (TFE) of apomyoglobin (AMb) from pure water into aqueous solution with trimethylamine N-oxide (TMAO) was investigated by all-atom molecular dynamics (MD) simulation combined with the Kirkwood-Buff (KB) integral method. The simulated TFE and the preferential interaction parameter correlated favorably with experimental values. In addition, the time-resolved KB integral revealed that a significant fluctuation in the TFE arose from the alteration in TMAO solvation around AMb. Furthermore, spatial decomposition of the KB integrals revealed how the local elements of the TFE are spatially distributed around AMb. These results revealed the spatio-temporal characteristics of the protein TFE into the molecular crowding condition with TMAO.
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.
