Probing Globular Protein Self-Assembling Dynamics by Heterodyne Transient Grating Experiments

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 measuremen...

Full description

Saved in:
Bibliographic Details
Published in:Applied sciences 2019-01, Vol.9 (3), p.405
Main Authors: Catalini, Sara, Taschin, Andrea, Bartolini, Paolo, Foggi, Paolo, Torre, Renato
Format: Article
Language:English
Subjects:
Acoustic properties
Acoustic waves
Acoustics
Damping
Experiments
Hydration
Hydrogels
Lysozyme
Propagation
Propagation velocity
Protein folding
protein hydrogel
protein self-assembling
Proteins
Sol-gel processes
Solvents
Sound propagation
Spectroscopy
Spectrum analysis
Temperature
transient grating spectroscopy
ultrasonic sound propagation
Wave propagation
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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 self-assembling 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.
ISSN:2076-3417
2076-3417
DOI:10.3390/app9030405