کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9954169 | 1540195 | 2018 | 40 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Domain communication in Thermotoga maritima Arginine Binding Protein unraveled through protein dissection
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
PBSProtein dissectionRMSFITCPDBRMSDSBPDSCdiagnostic tool - ابزار تشخیصیBiosensor - بیوسنسورcircular dichroism - رنگ تابی دورانیphosphate buffer saline - فسفات بافر شورroot mean square deviation - میانگین انحراف مربع ریشهroot mean square fluctuation - نوسان میانگین مربع ریشهProtein Data Bank - پروتئین بانک اطلاعاتیIsothermal titration calorimetry - کالری سنجی تیتاسیون ایزوترمالDifferential scanning calorimetry - کالریمتری روبشی افتراقی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Domain communication in Thermotoga maritima Arginine Binding Protein unraveled through protein dissection Domain communication in Thermotoga maritima Arginine Binding Protein unraveled through protein dissection](/preview/png/9954169.png)
چکیده انگلیسی
Substrate binding proteins represent a large protein family that plays fundamental roles in selective transportation of metabolites across membrane. The function of these proteins relies on the relative motions of their two domains. Insights into domain communication in this class of proteins have been here collected using Thermotoga maritima Arginine Binding Protein (TmArgBP) as model system. TmArgBP was dissected into two domains (D1 and D2) that were exhaustively characterized using a repertoire of different experimental and computational techniques. Indeed, stability, crystalline structure, ability to recognize the arginine substrate, and dynamics of the two individual domains have been here studied. Present data demonstrate that, although in the parent protein both D1 and D2 cooperate for the arginine anchoring; only D1 is intrinsically able to bind the substrate. The implications of this finding on the mechanism of arginine binding and release by TmArgBP have been discussed. Interestingly, both D1 and D2 retain the remarkable thermal/chemical stability of the parent protein. The analysis of the structural and dynamic properties of TmArgBP and of the individual domains highlights possible routes of domain communication. Finally, this study generated two interesting molecular tools, the two stable isolated domains that could be used in future investigations.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 119, November 2018, Pages 758-769
Journal: International Journal of Biological Macromolecules - Volume 119, November 2018, Pages 758-769
نویسندگان
Giovanni Smaldone, Nicole Balasco, Marilisa Vigorita, Alessia Ruggiero, Serena Cozzolino, Rita Berisio, Pompea Del Vecchio, Giuseppe Graziano, Luigi Vitagliano,