Abstract
Proteins are known to undergo denaturation and form different phases with varying physicochemical parameters. We report unusual stability of bovine serum albumin protein against commonly used denaturants (temperature and surfactant) in the charged reversal reentrant phase, caused by the multivalent counterions. Unlike monovalent counterions, which promote the denaturants' induced protein unfolding, the unfolding is restricted in the presence of multivalent ions. The observations are beyond the scope of general understanding of protein unfolding and are believed to be governed by ion-ion correlations driven strong condensation of the multivalent ions.
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.
