Issue 10, 2016

Orientation of polar molecules near charged protein interfaces

Abstract

We study the orientation of water and urea molecules and protein amide vibrations at aqueous α-lactalbumin and α-lactalbumin/urea interfaces using heterodyne-detected vibrational sum frequency generation. We vary the net charge of the protein by changing the pH. We find that the orientation of the water and urea molecules closely follows the net charge of the protein at the surface of the solution. In contrast, the net orientation of the amide groups of the backbone of the protein is independent of pH. We discuss the implications of these results for the mechanism by which urea denatures proteins.

Graphical abstract: Orientation of polar molecules near charged protein interfaces

Supplementary files

Article information

Article type
Paper
Submitted
20 Oct 2015
Accepted
11 Feb 2016
First published
11 Feb 2016

Phys. Chem. Chem. Phys., 2016,18, 7414-7418

Orientation of polar molecules near charged protein interfaces

S. Strazdaite, K. Meister and H. J. Bakker, Phys. Chem. Chem. Phys., 2016, 18, 7414 DOI: 10.1039/C5CP06372H

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