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  • The Role of Semidisorder in Temperature Adaptation of Bacterial FlgM Proteins

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    Author(s)
    Wang, Jihua
    Yang, Yuedong
    Cao, Zanxia
    Li, Zhixiu
    Zhao, Huiying
    Zhou, Yaoqi
    Griffith University Author(s)
    Zhou, Yaoqi
    Yang, Yuedong
    Li, Zhixiu
    Year published
    2013
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    Abstract
    Probabilities of disorder for FlgM proteins of 39 species whose optimal growth temperature ranges from 273 K (0é to 368 K (95é were predicted by a newly developed method called Sequence-based Prediction with Integrated NEural networks for Disorder (SPINE-D). We showed that the temperature-dependent behavior of FlgM proteins could be separated into two subgroups according to their sequence lengths. Only shorter sequences evolved to adapt to high temperatures (>318 K or 45é. Their ability to adapt to high temperatures was achieved through a transition from a fully disordered state with little secondary structure to a semidisordered ...
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    Probabilities of disorder for FlgM proteins of 39 species whose optimal growth temperature ranges from 273 K (0é to 368 K (95é were predicted by a newly developed method called Sequence-based Prediction with Integrated NEural networks for Disorder (SPINE-D). We showed that the temperature-dependent behavior of FlgM proteins could be separated into two subgroups according to their sequence lengths. Only shorter sequences evolved to adapt to high temperatures (>318 K or 45é. Their ability to adapt to high temperatures was achieved through a transition from a fully disordered state with little secondary structure to a semidisordered state with high predicted helical probability at the N-terminal region. The predicted results are consistent with available experimental data. An analysis of all orthologous protein families in 39 species suggests that such a transition from a fully disordered state to semidisordered and/or ordered states is one of the strategies employed by nature for adaptation to high temperatures.
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    Journal Title
    Biophysical Journal
    Volume
    105
    Issue
    11
    DOI
    https://doi.org/10.1016/j.bpj.2013.10.026
    Copyright Statement
    © 2013 Biophysical Society. The attached file is reproduced here in accordance with the copyright policy of the publisher. Please refer to the journal's website for access to the definitive, published version.
    Subject
    Physical sciences
    Biological physics
    Chemical sciences
    Biological sciences
    Publication URI
    http://hdl.handle.net/10072/56969
    Collection
    • Journal articles

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