Crystal structure of an insect antifreeze protein 1 Crystal Structure of an Insect Antifreeze Protein and its Implications for Ice Binding*
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چکیده
1 Department of Molecular Biophysics & Biochemistry, Yale University, New Haven, CT 06520 2 Department of Molecular, Cellular & Developmental Biology, Yale University, New Haven, CT 06520 3 Department of Biomedical & Molecular Sciences, Queen’s University, Kingston, ON K7L 3N6, Canada 4 Systems Biology Institute, Yale University, West Haven, CT 06516 5 These authors contributed equally to the work
منابع مشابه
Crystal structure of an insect antifreeze protein and its implications for ice binding.
Antifreeze proteins (AFPs) help some organisms resist freezing by binding to ice crystals and inhibiting their growth. The molecular basis for how these proteins recognize and bind ice is not well understood. The longhorn beetle Rhagium inquisitor can supercool to below -25 °C, in part by synthesizing the most potent antifreeze protein studied thus far (RiAFP). We report the crystal structure o...
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Insect antifreeze proteins (AFP) are much more effective than fish AFPs at depressing solution freezing points by ice-growth inhibition. AFP from the beetle Tenebrio molitor is a small protein (8.4 kDa) composed of tandem 12-residue repeats (TCTxSxxCxxAx). Here we report its 1.4-A resolution crystal structure, showing that this repetitive sequence translates into an exceptionally regular beta-h...
متن کاملWhy does insect antifreeze protein from Tenebrio molitor produce pyramidal ice crystallites?
The antifreeze protein (AFP) reduces the growth rates of the ice crystal facets. In that process the ice morphology undergoes a modification. An AFP-induced surface pinning mechanism, through matching of periodic bond chains in two dimensions, enables two-dimensional regular ice-binding surfaces (IBSs) of the insect AFPs to engage a certain class of ice surfaces, called primary surfaces. They a...
متن کاملA theoretical model of a plant antifreeze protein from Lolium perenne.
Antifreeze proteins (AFPs), found in certain organisms enduring freezing environments, have the ability to inhibit damaging ice crystal growth. Recently, the repetitive primary sequence of the AFP of perennial ryegrass, Lolium perenne, was reported. This macromolecular antifreeze has high ice recrystallization inhibition activity but relatively low thermal hysteresis activity. We present here a...
متن کاملStructural basis of antifreeze activity of a bacterial multi-domain antifreeze protein
Antifreeze proteins (AFPs) enhance the survival of organisms inhabiting cold environments by affecting the formation and/or structure of ice. We report the crystal structure of the first multi-domain AFP that has been characterized. The two ice binding domains are structurally similar. Each consists of an irregular β-helix with a triangular cross-section and a long α-helix that runs parallel on...
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تاریخ انتشار 2013