کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1927283 | 1536513 | 2006 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Fluorescence labeling and computational analysis of the strut of myosin's 50Â kDa cleft
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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
A new fluorescent labeling procedure specific for the strut sequence of myosin subfragment-1's 50Â kDa cleft was developed using CY3 N-hydroxy succinimidyl ester as a hydrophobic tag and hydrophobic interaction chromatography to purify the major labeled species which retained actin-activated ATPase activity. Stern-Volmer analysis suggests that the CY3 is in close proximity to basic residues, consistent with inspection of the mapped labeling site in the atomic model. Fluorescence polarization indicates that the CY3 becomes more mobile upon actin binding, supporting a location near the actomyosin interface. In contrast, nucleotide binding to myosin had little impact on the CY3. Molecular mechanics and stochastic dynamics simulations suggest that this labeling site is sensitive to forced cleft opening and closure, but the upper 50Â kDa cleft does not move easily. In addition, there appear to be some long-range effects of forced cleft opening and closing that could impact the lever arm position.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volume 456, Issue 2, 15 December 2006, Pages 102-111
Journal: Archives of Biochemistry and Biophysics - Volume 456, Issue 2, 15 December 2006, Pages 102-111
نویسندگان
Ravi Kumar Gawalapu, Douglas D. Root,