Abstract
The concentration dependences of self-diffusion coefficient for intrinsically disordered milk protein αS-casein were studied by pulsed field gradient nuclear magnetic resonance. The experimental data were analyzed in a view of phenomenological approach based on the frictional formalism of non-equilibrium thermodynamics by Vink. The results of αS-CN hydrodynamic study showed that at low- and high-protein concentrations, αS-CN exists in the different structural forms. At low concentrations in the rather broad concentration range, protein remains monomeric but with greater hydrodynamic size than have rigid globular proteins of the equal mass. At high concentrations beyond the definite protein content, αS-CN tends to form associates. The application of the Vink’s approach to αS-CN testifies that the role of flexible domains in the process of self-diffusion is mainly in increasing the friction of between αS-CN molecules due to their inter-entanglement. The latter physically means that when αS-CN molecules cling each other by their flexible domains, this phenomenon provides much more efficient friction than their interaction with solvent molecules.
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.
