کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
5191007 1381223 2006 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
The unfolding and folding dynamics of TNfnALL probed by single molecule force-ramp spectroscopy
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آلی
پیش نمایش صفحه اول مقاله
The unfolding and folding dynamics of TNfnALL probed by single molecule force-ramp spectroscopy
چکیده انگلیسی
Tenascin, an important extracellular matrix protein, is subject to stretching force under physiological conditions and plays important roles in regulating the cell-matrix interactions. Using the recently developed single molecule force-ramp spectroscopy, we investigated the unfolding-folding kinetics of a recombinant tenascin fragment TNfnALL. Our results showed that all the 15 FnIII domains in TNfnALL have similar spontaneous unfolding rate constant at zero force, but show great difference in their folding rate constants. Our results demonstrated that single molecule force-ramp spectroscopy is a powerful tool for accurate determination of the kinetic parameters that characterize the unfolding and folding reactions. We anticipate that single molecule force-ramp spectroscopy will become a versatile addition to the single molecule manipulation tool box and greatly expand the scope of single molecule force spectroscopy.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Polymer - Volume 47, Issue 7, 22 March 2006, Pages 2548-2554
نویسندگان
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