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Small angle neutron scattering study on the structural variation of lysozyme in bioprotectants

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Abstract

The thermal denaturation and subsequent structural variation of lysozyme in various bioprotectant candidate solutions such as trehalose and choline acetate have been investigated by using small angle neutron scattering and differential scanning calorimetry. The gyration radius shows little change with the addition of additives in a native state at room temperature. On heating the lysozyme solution, a remarkable increase in the gyration radius is observed at temperatures above the denaturation temperature without any bioprotectants. Such an increase is suppressed by the additives owing to the intermolecular interactions between the lysozyme molecules and the bioprotectants of trehalose and choline acetate. The fractal dimension of lysozyme varies slightly with the addition of the bioprotectant solutions, and shows a remarkable drop in the vicinity of the denaturation temperature for all the solutions.

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Authors and Affiliations

  1. Graduate School of Pure and Applied Sciences, University of Tsukuba, Ibaraki, 305-8573, Japan

    Shota Koda, Haruki Takayama, Tomohiko Shibata, Tatsuya Mori & Seiji Kojima

  2. Institute of Nano Science and Technology, Hanyang University, Seoul, 133-791, Korea

    In-Sung Park

  3. Neutron Science Division, Korea Atomic Energy Research Institute, Daejeon, 305-353, Korea

    Tae-Gyu Shin

Authors
  1. Shota Koda
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  2. Haruki Takayama
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  3. Tomohiko Shibata
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  4. Tatsuya Mori
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  5. Seiji Kojima
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  6. In-Sung Park
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  7. Tae-Gyu Shin
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Correspondence to Shota Koda.

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Koda, S., Takayama, H., Shibata, T. et al. Small angle neutron scattering study on the structural variation of lysozyme in bioprotectants. Journal of the Korean Physical Society 66, 1376–1380 (2015). https://doi.org/10.3938/jkps.66.1376

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  • DOI: https://doi.org/10.3938/jkps.66.1376

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