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AntWatFre

Hydration Dynamics of Antifreeze Proteins

Total Cost €

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EC-Contrib. €

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Partnership

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Project "AntWatFre" data sheet

The following table provides information about the project.

Coordinator
STICHTING NEDERLANDSE WETENSCHAPPELIJK ONDERZOEK INSTITUTEN 

Organization address
address: WINTHONTLAAN 2
city: UTRECHT
postcode: 3526 KV
website: www.fom.nl

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country Netherlands [NL]
 Project website http://www.amolf.nl
 Total cost 165˙598 €
 EC max contribution 165˙598 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2014
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2015
 Duration (year-month-day) from 2015-11-01   to  2017-10-31

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    STICHTING NEDERLANDSE WETENSCHAPPELIJK ONDERZOEK INSTITUTEN NL (UTRECHT) coordinator 165˙598.00

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 Project objective

Antifreeze proteins (AFPs) and antifreeze glycoproteins (AFGPs) enable the survival of various organisms in freezing or subfreezing habitats. Even millimolar concentrations of these proteins are sufficient to lower the freezing temperature by several degrees. To reach a similar freezing point depression using sodium chloride would require molar concentrations. Nowadays AF(G)Ps already find applications in food industry, for instance to prevent recrystallization in ice cream and have great potential in medical applications (cell & organ storage, operations at low temperature). Protein-water interactions are of general interest owing to the importance of protein hydration for protein function; AF(G)Ps form an extraordinary example of this coupling that is sufficiently strong and specific that the protein controls macroscopic thermodynamic properties of water. Despite their importance in nature and their industrial relevance, the mechanisms by which AF(G)Ps depress the freezing point are still poorly understood. Although substantial information presently exists on the static protein structures and thermodynamic properties of these systems, molecular scale information on the dynamics of the conformations of the AF(G)Ps, their hydration shells and their binding to ice, is extremely scarce. Here we propose to study the molecular mechanisms by which AF(G)Ps lower the freezing temperature with advanced nonlinear spectroscopic techniques like 2D polarization-resolved vibrational spectroscopy and surface sum-frequency generation. These techniques enable the label-free study of the structural dynamics of the AF(G)P conformations, their hydration shells and their mechanism of binding to the ice surface. They will be used to study several key elements in the functioning of AF(G)Ps.

 Publications

year authors and title journal last update
List of publications.
2016 Patrick Balzerowski, Konrad Meister, Jan Versluis, Huib J. Bakker
Heterodyne-detected sum frequency generation spectroscopy of polyacrylic acid at the air/water-interface
published pages: 2481-2487, ISSN: 1463-9076, DOI: 10.1039/c5cp06177f
Phys. Chem. Chem. Phys. 18/4 2019-06-13
2016 Simona Strazdaite, Konrad Meister, Huib J. Bakker
Orientation of polar molecules near charged protein interfaces
published pages: 7414-7418, ISSN: 1463-9076, DOI: 10.1039/c5cp06372h
Phys. Chem. Chem. Phys. 18/10 2019-06-13
2016 Luuk L. C. Olijve, Konrad Meister, Arthur L. DeVries, John G. Duman, Shuaiqi Guo, Huib J. Bakker, Ilja K. Voets
Blocking rapid ice crystal growth through nonbasal plane adsorption of antifreeze proteins
published pages: 3740-3745, ISSN: 0027-8424, DOI: 10.1073/pnas.1524109113
Proceedings of the National Academy of Sciences 113/14 2019-06-13

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