کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1987180 | 1540274 | 2012 | 4 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
GTP binds to α-crystallin and causes a significant conformational change
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
ATP was previously reported to bind to the chaperone α-crystallin resulting in a significant effect on the protein's ability to suppress the aggregation of a thermally denatured protein. Here, we have investigated the binding of GTP to α-crystallin. Unlike ATP, binding of GTP to α-crystallin did not affect its ability to suppress the aggregation of thermally denatured rhodanese. GTP binding induced a conformational change on α-crystallin, however the degree of exposed hydrophobic surfaces, which are believed to be involved in the binding of the chaperone to denaturing proteins did not change. Here, we report that GTP binds to α-crystallin and this results in a decreased stability of the chaperone as indicated by urea denaturation.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 50, Issue 4, 1 May 2012, Pages 895–898
Journal: International Journal of Biological Macromolecules - Volume 50, Issue 4, 1 May 2012, Pages 895–898
نویسندگان
Jose A. Mendoza, Matthew D. Correa, Gustavo Zardeneta,