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Probing Molecular Dynamics Surrounding a Type I Ice-Binding Protein in Water and Anti-icing Fluids through Variable Temperature Dependent Site-Directed Spin Labeling EPR Technique
Başlık:
Probing Molecular Dynamics Surrounding a Type I Ice-Binding Protein in Water and Anti-icing Fluids through Variable Temperature Dependent Site-Directed Spin Labeling EPR Technique
Yazar:
Flores, Antonia, author.
ISBN:
9780438069008
Yazar Ek Girişi:
Fiziksel Tanımlama:
1 electronic resource (167 pages)
Genel Not:
Source: Masters Abstracts International, Volume: 57-06M(E).
Advisors: Yong Ba Committee members: Karin E. Brown; Andre Ellis.
Özet:
Ice-binding proteins (IBPs) are a class of polypeptides produced by specific organisms to prevent cell damage due to the freezing of body fluids in subzero environments. IBPs inhibit the growth of ice by binding to specific surfaces of seed ice crystals. Many studies have examined IBPs' structures and functions; however, the mechanism of action at molecular level has remained unclear. This study applied site-directed spin labeling (SDSL) Electron Paramagnetic Resonance (EPR) technique to gain molecular insight into the dynamics and interactions of the selected peptide side chains with water molecules in the Water-IBP-Ice interfacial region. The effects of IBPs on the freezing, melting kinetics, and thermodynamics of water and the deicing/anti-icing fluids were studied using cryo-optical micro-imaging methods. Also, the local freezing point surrounding spin-labeled IBPs were examined by EPR experiments. We confirmed the ice binding surface of Type I IBP. VT-EPR spectra showed that the spin labeled IBPs inhibit the nucleation of ice crystals in their aqueous solution. Additionally, the VT EPR spectral line-shapes of the spin-labeled IBPs at different residues reveal that Type I IBP molecules might stay in the water as dimers (through the dynamic binding of the two hydrophobic ice binding surfaces). This phenomenon demonstrates why water's solubilities of Type I IBPs are so high even they have numerous hydrophobic Ala residues in the peptides. Also, the VT EPR spectra showed that the IBP molecules and liquid-like water molecules formed dense layers between ice sheets in the frozen bulk solutions at very low subzero temperatures. This event eventually induced bulk melting of the ice matrices at increased subzero temperatures. These experimental results allow for future study to apply IBPs as an active ingredient to make environmentally friendly deicing/anti-icing fluids.
Notlar:
School code: 0962
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Yer Numarası | Demirbaş Numarası | Shelf Location | Lokasyon / Statüsü / İade Tarihi |
---|---|---|---|
XX(687939.1) | 687939-1001 | Proquest E-Tez Koleksiyonu | Arıyor... |
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