Orientation of polar molecules near charged protein interfaces

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 w...

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Bibliographic Details
Published in:Physical chemistry chemical physics : PCCP 2016-03, Vol.18 (1), p.7414-7418
Main Authors: Strazdaite, Simona, Meister, Konrad, Bakker, Huib J
Format: Article
Language:English
Subjects:
Amides
Charge
Charging
Orientation
Proteins
Proteins - chemistry
Urea - chemistry
Ureas
Vibration
Water - chemistry
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Summary: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. 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.
ISSN:1463-9076
1463-9084
DOI:10.1039/c5cp06372h