Abstract
The mechanism of denaturation of human serum albumin under action of an anionic detergent – sodium dodecyl sulfate (SDS) is investigated by Raman spectroscopy method. The quantitative contents of α-helical segments and random packing segments of polypeptide chain of albumin at different concentrations of SDS and at different pH values of solutions are determined. It is shown, that more intensive denaturation under action of SDS, consisting in disturbance of secondary and tertiary structure of albumin, takes place at pH values of solution, smaller the isoelectric point of protein.
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.
