Abstract
The effect of putrescine on the dynamics, conformation, and kinetics of acid phosphatase investigated via different experimental and theoretical methods. The Stern-Volmer constants (Ksv) for the acid phosphatase- putrescine compound was obtained at different temperatures. Therefore, putrescine quenched the intensity of the enzyme via the static method. Gibbs free energy displayed which binding process was spontaneous. MD simulation, docking method, and thermodynamic parameters revealed the van der Waals forces and hydrogen bonding that had the specific interaction in unfolding the compound. After putrescine binding, the Vmax amounts of acid phosphatase without changed, and the value of kcat/Km increased. The Tm the acid phosphatase-putrescine compound was decreased. Presumably because of more surface hydrophilicity and further H-bond formation underlying the putrescine modification. As confirmed by fluorescence spectra and UV–Visible spectroscopy. Circular dichroism (CD) and UV absorption investigations also demonstrated which binding of putrescine to acid phosphatase led to microenvironmental variations around the protein. Therefore, putrescine cause changes in its structure and function. The results, therefore, showed the effect of putrescine was because of its kosmotropic specifications. Molecular dynamics simulation and Molecular docking results further confirmed the results obtained by CD and spectroscopy experiments.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
More From: International Journal of Biological Macromolecules
Disclaimer: 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.