Probing globular protein self-assembling dynamics by heterodyne transient grating experiments
Authors: Catalini S., Taschin A., Bartolini P., Foggi P., Torre R.
Autors Affiliation: European Laboratory for Non-Linear Spectroscopy (LENS), Università di Firenze, Florence, 50121, Italy; Dip. di Fisica ed Astronomia, Università di Firenze, Florence, 50121, Italy; Dip. di Chimica, Biologia e Biotecnologie, Università di Perugia, Perugia, Italy
Abstract: In this work, we studied the propagation of ultrasonic waves of lysozyme solutions characterized by different degrees of aggregation and networking. The experimental investigation was performed by means of the transient grating (TG) spectroscopy as a function of temperature, which enabled measurement of the ultrasonic acoustic proprieties over a wide time window, ranging from nanoseconds to milliseconds. The fitting of the measured TG signal allowed the extraction of several dynamic properties, here we focused on the speed and the damping rate of sound. The temperature variation induced a series of processes in the lysozyme solutions: Protein folding-unfolding, aggregation and sol-gel transition. Our TG investigation showed how these selfassembling phenomena modulate the sound propagation, affecting both the velocity and the damping rate of the ultrasonic waves. In particular, the damping of ultrasonic acoustic waves proved to be a dynamic property very sensitive to the protein conformational rearrangements and aggregation processes.
Journal/Review: APPLIED SCIENCES-BASEL
Volume: 9 (3) Pages from: 405-1 to: 405-11
More Information: This research was funded by Ente Cassa di Risparmio Firenze, 2016-0866 and European Community by Laserlab-Europe, H2020 EC-GA-654148.KeyWords: Lysozyme; Protein hydrogel; Protein self-assembling; Transient grating spectroscopy; Ultrasonic sound propagationDOI: 10.3390/app9030405Citations: 2data from “WEB OF SCIENCE” (of Thomson Reuters) are update at: 2021-10-17References taken from IsiWeb of Knowledge: (subscribers only)Connecting to view paper tab on IsiWeb: Click hereConnecting to view citations from IsiWeb: Click here