An Antifreeze Protein Folds with an Interior Network of More Than 400 Semi-Clathrate Waters

Sun, Tianjun; Lin, Feng-Hsu; Campbell, Robert L.; Allingham, John S.; Davies, Peter L.

doi:10.1126/science.1247407

Cited by 163 publications

(178 citation statements)

References 34 publications

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“…2(i) and 2(ii)]. 47,48 In contrast, type II and III fish AFPs are nonrepetitive and show an overall globular fold. 49,50 In fish type II AFPs, this fold is stabilized by cysteine residues.…”

Section: Structure Of Ice-binding Proteinsmentioning

confidence: 99%

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Interaction of ice binding proteins with ice, water and ions

et al. 2016

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Articles you may be interested inExplicit-water theory for the salt-specific effects and Hofmeister series in protein solutions J. Chem. Phys. 144, 215101 (2016) Ice binding proteins (IBPs) are produced by various cold-adapted organisms to protect their body tissues against freeze damage. First discovered in Antarctic fish living in shallow waters, IBPs were later found in insects, microorganisms, and plants. Despite great structural diversity, all IBPs adhere to growing ice crystals, which is essential for their extensive repertoire of biological functions. Some IBPs maintain liquid inclusions within ice or inhibit recrystallization of ice, while other types suppress freezing by blocking further ice growth. In contrast, ice nucleating proteins stimulate ice nucleation just below 0 C. Despite huge commercial interest and major scientific breakthroughs, the precise working mechanism of IBPs has not yet been unraveled. In this review, the authors outline the state-of-the-art in experimental and theoretical IBP research and discuss future scientific challenges. The interaction of IBPs with ice, water and ions is examined, focusing in particular on ice growth inhibition mechanisms.

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Section: Structure Of Ice-binding Proteinsmentioning

confidence: 99%

“…Despite this lack regularity in the IBS these proteins are able to bind both basal and prism planes. [59][60][61]65 Crystal structures of various AFPs reveal ordered waters associated with the protein IBS, 48,56,58,65 which are thought to play an important role in ice-binding (see Sec. VI E for more details).…”

Section: -58mentioning

confidence: 99%

Interaction of ice binding proteins with ice, water and ions

et al. 2016

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“…Possibly, the adsorption of PVA onto ice surfaces is promoted via an indirect interaction of clathrate waters hydrogen-bonded to the hydroxyl groups of the polymer, similar to the binding mechanism of antifreeze proteins to ice surfaces. [30][31][32] Further investigation of the specifi c hydration of PVA may shed light on the adsorption mechanism of PVA onto ice surfaces.…”

Section: Implications For the Ice Binding Of Pvamentioning

confidence: 99%

Influence of Polymer Chain Architecture of Poly(vinyl alcohol) on the Inhibition of Ice Recrystallization

Olijve

Hendrix

Voets

2016

Macromol. Chem. Phys.

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Poly(vinyl alcohol) (PVA) is a water‐soluble synthetic polymer well‐known to effectively block the recrystallization of ice. The effect of polymer chain architecture on the ice recrystallization inhibition (IRI) by PVA remains unexplored. In this work, the synthesis of PVA molecular bottlebrushes is described via a combination of atom‐transfer radical polymerization and reversible addition‐fragmentation chain‐transfer polymerization. The facile preparation of the PVA bottlebrushes is performed via the selective hydrolysis of the chloroacetate esters of the poly(vinyl chloroacetate) (PVClAc) side chains of a PVClAc precursor bottlebrush. The IRI efficacy of the PVA bottlebrush is quantitatively compared to linear PVA. The results show that even if the PVA chains are densely grafted onto a rigid polymer backbone, the IRI activity of PVA is maintained, demonstrating the flexibility in PVA polymer chain architecture for the design of synthetic PVA‐based ice growth inhibitors.

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“…When these protein-bound waters contact the quasi-liquid layer at the interface with ice, the two ice-like water arrangements could fuse together and then turn to ice at temperatures in the TH range. Structure-function analyses have shown that AFPs collectively have a variety of different surfaces (ice-binding sites) that can organize water molecules into a clathrate (8,9).…”

mentioning

confidence: 99%

Flies expand the repertoire of protein structures that bind ice

Basu

Graham

Campbell

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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An antifreeze protein (AFP) with no known homologs has been identified in Lake Ontario midges (Chironomidae). The midge AFP is expressed as a family of isoforms at low levels in adults, which emerge from fresh water in spring before the threat of freezing temperatures has passed. The 9.1-kDa major isoform derived from a preproprotein precursor is glycosylated and has a 10-residue tandem repeating sequence xxCxGxYCxG, with regularly spaced cysteines, glycines, and tyrosines comprising one-half its 79 residues. Modeling and molecular dynamics predict a tightly wound left-handed solenoid fold in which the cysteines form a disulfide core to brace each of the eight 10-residue coils. The solenoid is reinforced by intrachain hydrogen bonds, side-chain salt bridges, and a row of seven stacked tyrosines on the hydrophobic side that forms the putative ice-binding site. A disulfide core is also a feature of the similar-sized beetle AFP that is a β-helix with seven 12-residue coils and a comparable circular dichroism spectrum. The midge and beetle AFPs are not homologous and their ice-binding sites are radically different, with the latter comprising two parallel arrays of outward-pointing threonines. However, their structural similarities is an amazing example of convergent evolution in different orders of insects to cope with change to a colder climate and provide confirmation about the physical features needed for a protein to bind ice.

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An Antifreeze Protein Folds with an Interior Network of More Than 400 Semi-Clathrate Waters

Cited by 163 publications

References 34 publications

Interaction of ice binding proteins with ice, water and ions

Interaction of ice binding proteins with ice, water and ions

Influence of Polymer Chain Architecture of Poly(vinyl alcohol) on the Inhibition of Ice Recrystallization

Flies expand the repertoire of protein structures that bind ice

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