کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1987197 1540274 2012 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Calcium-induced changes in calmodulin structural dynamics and thermodynamics
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Calcium-induced changes in calmodulin structural dynamics and thermodynamics
چکیده انگلیسی

The thermodynamics of the interaction between Ca2+ and calmodulin (CaM) was examined using isothermal titration calorimetry (ITC). The chemical denaturation of calmodulin was monitored spectroscopically to determine the stability of Ca2+-free (apo) and Ca2+-loaded (holo) CaMs. We explored the conformational and structural dynamics of CaM using amide hydrogen–deuterium (H–D) exchange coupled with Fourier transform infrared (FT-IR) spectroscopy. The results of H–D exchange and FT-IR suggest that CaM activation by Ca2+ binding involves significant conformational changes. The results have also revealed that while the overall conformation of holo-CaM is more stable than that of the apo-CaM, some part of its α-helix structures, most likely the EF-hand domain region, has more solvent exposure, thus, has a faster H–D exchange rate than that of the apo-CaM. The ITC method provides a new strategy for obtaining site-specific Ca2+ binding properties and a better estimation of the cooperativity and conformational change contributions of coupled EF-hand proteins.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 50, Issue 4, 1 May 2012, Pages 1011–1017
نویسندگان
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