کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8648253 | 1570441 | 2018 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Comparative mechanical unfolding studies of spectrin domains R15, R16 and R17
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شناسی مولکولی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Comparative mechanical unfolding studies of spectrin domains R15, R16 and R17 Comparative mechanical unfolding studies of spectrin domains R15, R16 and R17](/preview/png/8648253.png)
چکیده انگلیسی
Spectrins belong to repetitive three-helix bundle proteins that have vital functions in multicellular organisms and are of potential value in nanotechnology. To reveal the unique physical features of repeat proteins we have studied the structural and mechanical properties of three repeats of chicken brain α-spectrin (R15, R16 and R17) at the atomic level under stretching at constant velocities (0.01, 0.05 and 0.1â¯Ã
·psâ1) and constant forces (700 and 900â¯pN) using molecular dynamics (MD) simulations at Tâ¯=â¯300â¯K. 114 independent MD simulations were performed and their analysis has been done. Despite structural similarity of these domains we have found that R15 is less mechanically stable than R16, which is less stable than R17. This result is in agreement with the thermal unfolding rates. Moreover, we have observed the relationship between mechanical stability, flexibility of the domains and the number of aromatic residues involved in aromatic clusters.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Structural Biology - Volume 201, Issue 2, February 2018, Pages 162-170
Journal: Journal of Structural Biology - Volume 201, Issue 2, February 2018, Pages 162-170
نویسندگان
Anna V. Glyakina, Ilya V. Likhachev, Nikolay K. Balabaev, Oxana V. Galzitskaya,