Ice-binding site of surface-bound type III antifreeze protein partially decoupled from water
Author:
Affiliation:
1. Department of Chemistry
2. Aarhus University
3. 8000 Aarhus C
4. Denmark
5. Department of Chemical Engineering
6. University of Washington
7. Seattle
8. USA
9. Indian Institute of Technology
10. Roorkee 247667
11. India
Abstract
Combined SFG/MD analysis together with spectral calculations revealed that type III antifreeze proteins adsorbed at the air–water interface maintains a native state and adopts an orientation that leads to a partial decoupling of its ice-binding site from water.
Funder
Division of Graduate Education
Deutsche Forschungsgemeinschaft
Aarhus Universitets Forskningsfond
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://pubs.rsc.org/en/content/articlepdf/2018/CP/C8CP03382J
Reference59 articles.
1. Antifreeze Proteins from Diverse Organisms and their Applications: An Overview
2. Ice-binding proteins: a remarkable diversity of structures for stopping and starting ice growth
3. Adsorption inhibition as a mechanism of freezing resistance in polar fishes.
4. Inhibition of growth of nonbasal planes in ice by fish antifreezes.
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