ملخص
Attenuated total reflection Fourier transform infrared (ATR-FTIR) spectroscopy using a special waveguide based on a silver halide fiber was used for probing the heat-induced secondary structure and conformation changes of bovine serum albumin (BSA). From the secondary derivative and the curve fitting of the obtained ATR-FTIR spectra, the changes of the BSA secondary structure with temperature were clearly identified. Two different thermal denaturation temperature ranges (i.e., 50-52 and 80-82°C, at which a change of the protein structure occurred) were determined, while only one denaturation temperature was previously identified via classical FTIR measurements. Additionally, taking advantage of two-dimensional correlation spectroscopy more detailed information on changes of the protein secondary structure was revealed. The developed method facilitates in situ, sensitive, and more in-depth probing of protein secondary structures, which represents a significant advancement compared to conventional characterization methods.
اللغة الأصلية | الإنجليزيّة |
---|---|
الصفحات (من إلى) | 765-770 |
عدد الصفحات | 6 |
دورية | The Analyst |
مستوى الصوت | 140 |
رقم الإصدار | 3 |
المعرِّفات الرقمية للأشياء | |
حالة النشر | نُشِر - 7 فبراير 2015 |