Abstract
The structure of biological molecules plays an important role in many biological processes. The variation of ambient parameters such as pH, temperature or pressure can influence important properties of protein molecules like conformation or stability. By means of the perturbed angular correlation (PAC) technique and atomic force microscopy (AFM) a conformation change of bovine serum albumin (BSA) molecules has been studied as a function of the pH value of the BSA solution. The observed decrease of the rotational correlation time and the increase of molecule diameter as a function of pH were attributed to conformational changes of bovine serum albumin induced by different pH values of the BSA solution.
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.
