کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2052668 | 1074235 | 2006 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Hyper-thermostability of CutA1 protein, with a denaturation temperature of nearly 150 °C
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Hyper-thermostability of CutA1 protein, with a denaturation temperature of nearly 150 °C Hyper-thermostability of CutA1 protein, with a denaturation temperature of nearly 150 °C](/preview/png/2052668.png)
چکیده انگلیسی
We found that the CutA1 protein, from Pyrococcus horikoshii (PhCutA1), has an extremely high denaturation temperature (Td) of nearly 150 °C, which exceeds the highest record determined by DSC by about 30 °C. To elucidate the mechanism of the ultra-high stability of PhCutA1, we analyzed the crystal structures of CutA1 proteins from three different sources, P. horikoshii, Thermus thermophilus, and Escherichia coli, with different growth temperatures (98, 75, and 37 °C). This analysis revealed that the remarkably increased number of ion pairs in the monomeric structure contributes to the stabilization of the trimeric structure and plays an important role in enhancing the Td, up to 150 °C, for PhCutA1.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 580, Issue 17, 24 July 2006, Pages 4224–4230
Journal: FEBS Letters - Volume 580, Issue 17, 24 July 2006, Pages 4224–4230
نویسندگان
Tomoyuki Tanaka, Masahide Sawano, Kyoko Ogasahara, Yasushi Sakaguchi, Bagautdin Bagautdinov, Etsuko Katoh, Chizu Kuroishi, Akeo Shinkai, Shigeyuki Yokoyama, Katsuhide Yutani,