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  • Title: Biophysical characterization of soluble Pseudomonas syringae ice nucleation protein InaZ fragments.
    Author: Han YJ, Song H, Lee CW, Ly NH, Joo SW, Lee JH, Kim SJ, Park S.
    Journal: Int J Biol Macromol; 2017 Jan; 94(Pt A):634-641. PubMed ID: 27773839.
    Abstract:
    Ice nucleation protein (INP) with its functional domain consisting of multiple 48-residue repeat units effectively induces super-cooled water into ice. Circular dichroism and infrared deconvolution analyses on a soluble 240-residue fragment of Pseudomonas syringae InaZ (InaZ240) containing five 48-residue repeat units indicated that it is mostly composed of β-sheet and random coil. Analytical ultracentrifugation suggested that InaZ240 behaves as a monomer of an elongated ellipsoid. However, InaZ240 showed only minimum ice binding compared to anti-freeze proteins. Other P. syringae InaZ proteins with more 48-residue repeat units were made, in which the largest soluble fragment obtainable was an InaZ with twelve 48-residue repeat units. Size-exclusion chromatography analyses further suggested that the overall shape of the expressed InaZ fragments is pH-dependent, which becomes compact as the numbers of 48-residue repeat unit increase.
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