کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10536786 | 962605 | 2015 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The thermal unfolding of the ribosome-inactivating protein saporin-S6 characterized by infrared spectroscopy
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کلمات کلیدی
2D-COSThermal unfolding - تابش گرماییFTIR - طیف سنج مادون قرمزInfrared spectroscopy - طیف سنجی مادون قرمزFourier transform infrared spectroscopy - طیف سنجی مادون قرمز تبدیل فوریه یا طیف سنجی FTIRTwo-dimensional correlation spectroscopy - طیف سنجی همبستگی دو بعدیRIP - پاره کردنRibosome-inactivating protein - پروتئین غیر فعال کننده ریبوزوم
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
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![عکس صفحه اول مقاله: The thermal unfolding of the ribosome-inactivating protein saporin-S6 characterized by infrared spectroscopy The thermal unfolding of the ribosome-inactivating protein saporin-S6 characterized by infrared spectroscopy](/preview/png/10536786.png)
چکیده انگلیسی
Saporin-S6 is a plant toxin belonging to the type 1 ribosome-inactivating protein (RIP) family. Since it was extracted and isolated from Saponaria officinalis for the first time almost thirty years ago, the protein has been widely studied mainly for its potential applications in anti-tumour and anti-viral infection therapy. Like other RIPs, saporin-S6 is particularly effective in the form of immunotoxin conjugated with monoclonal antibodies and its chemico-physical characteristics made the protein a perfect candidate for the synthesis, development and use of saporin-S6-based chimeric toxins. The high stability of the protein against different denaturing agents has been broadly demonstrated, however, its complete thermal unfolding characterization has not already been performed. In this work we analyse in detail structure, thermostability and unfolding features by means of infrared spectroscopy coupled with two-dimensional correlation spectroscopy. Our data showed that saporin-S6 in solution at neutral pH exhibits a secondary structure analogue to that of the crystal and confirmed its good stability at moderately high temperatures, with a temperature of melting of 58 °C. Our results also demonstrated that the thermal unfolding process is non-cooperative and occurs in two steps, and revealed the sequence of the events that take place during the denaturation, showing a higher stability of the N-terminal domain of the protein.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1854, Issue 10, Part A, October 2015, Pages 1357-1364
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1854, Issue 10, Part A, October 2015, Pages 1357-1364
نویسندگان
Marina Sánchez, Andrea Scirè, Fabio Tanfani, Alessio Ausili,