Direct Visualization of Spruce Budworm Antifreeze Protein Interacting with Ice Crystals: Basal Plane Affinity Confers Hyperactivity

Pertaya, Natalya; Marshall, Christopher B.; Celik, Yeliz; Davies, Peter L.; Braslavsky, Ido

doi:10.1529/biophysj.107.125328

Cited by 105 publications

(97 citation statements)

References 55 publications

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“…Indeed, it is this distance, seen in the β-helical AFPs, which closely matches the 4.5-Å critical repeating distance of oxygen atoms on both the primary prism and basal planes of ice (41). Binding to both these planes can explain hyperactivity (16,42). We predict that the Tyr ladder will play a role in ice binding through formation of clathrate waters around the phenyl groups with "anchoring" to the Tyr hydroxyls and backbone peptide groups.…”

Section: Discussionsupporting

confidence: 61%

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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Section: Discussionsupporting

confidence: 61%

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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“…Experiments were conducted using a custom-designed nanoliter osmometer, and samples were observed by confocal microscopy (15). We examined four hypAFPs and four moderate AFPs.…”

Section: Resultsmentioning

confidence: 99%

“…One factor that has been postulated to explain the difference in FH activity between hypAFPs and moderately active fish AFPs is that while both types bind to prism or pyramidal planes, only the former binds to the basal planes (13,15). Although ice growth or melting tends to be slower on the basal plane, a lack of binding to this surface could lead to easier melting of ice crystals (11).…”

Section: Discussionmentioning

confidence: 99%

Superheating of ice crystals in antifreeze protein solutions

Celik

Graham

Mok

et al. 2010

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

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125

126

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It has been argued that for antifreeze proteins (AFPs) to stop ice crystal growth, they must irreversibly bind to the ice surface. Surface-adsorbed AFPs should also prevent ice from melting, but to date this has been demonstrated only in a qualitative manner. Here we present the first quantitative measurements of superheating of ice in AFP solutions. Superheated ice crystals were stable for hours above their equilibrium melting point, and the maximum superheating obtained was 0.44°C. When melting commenced in this superheated regime, rapid melting of the crystals from a point on the surface was observed. This increase in melting temperature was more appreciable for hyperactive AFPs compared to the AFPs with moderate antifreeze activity. For each of the AFP solutions that exhibited superheating, the enhancement of the melting temperature was far smaller than the depression of the freezing temperature. The present findings clearly show that AFPs adsorb to ice surfaces as part of their mechanism of action, and this absorption leads to protection of ice against melting as well as freezing.Gibbs-Thomson effect | ice recrystallization | irreversible binding | melting hysteresis | thermal hysteresis

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“…26,27 However, the stability of binding to the ice crystal planes remains unclear. Moreover, it is almost impossible to conduct experimental analyses on the molecular-scale growth kinetics of ice around AFPs at the planes.…”

Section: Introductionmentioning

confidence: 99%

Antifreeze proteins: computer simulation studies on the mechanism of ice growth inhibition

Nada

Furukawa

2012

Polym J

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Antifreeze proteins (AFPs), which are present in the bodily fluids of organisms inhabiting cold environments, function as inhibitors of ice growth by binding to certain planes of ice crystals. However, the exact mechanism of ice growth inhibition is still poorly understood as it is exceedingly difficult to experimentally analyze the molecular-scale growth kinetics of ice crystals at the planes to which the proteins bind. This review paper focuses on computer simulation studies on the mechanism of ice growth inhibition by AFPs. Recent molecular dynamics simulations of a growing ice-water interface to which protein is bound have indicated that, when the protein is stably bound to the interface, the growth rate of ice surrounding the protein decreases drastically, owing to depression of the ice melting point through the Gibbs-Thomson effect. The observed decrease in growth rate is expected to correspond to ice growth inhibition in real-world systems. In addition to presenting published simulation studies on the mechanism of ice growth inhibition by AFPs, this review also outlines the direction of future simulation studies in this field.

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Direct Visualization of Spruce Budworm Antifreeze Protein Interacting with Ice Crystals: Basal Plane Affinity Confers Hyperactivity

Cited by 105 publications

References 55 publications

Flies expand the repertoire of protein structures that bind ice

Flies expand the repertoire of protein structures that bind ice

Superheating of ice crystals in antifreeze protein solutions

Antifreeze proteins: computer simulation studies on the mechanism of ice growth inhibition

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