کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9757452 | 1496004 | 2005 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
FTIR study on thermal denaturation and aggregation of recombinant hamster prion protein SHaPrP90-232
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
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چکیده انگلیسی
We have investigated the temperature induced denaturation and aggregation of the recombinant fragment SHaPrP90-232 of the hamster prion protein by Fourier transform infrared (FTIR) spectroscopy in H2O and D2O buffers. Difference spectra of this denaturation/aggregation reaction revealed a decrease of α-helical and turn structures and an increase of intermolecularly formed antiparallel β-sheet structure. Compared to previously examined critical oligomers in H2O buffer, the temperature induced aggregates of SHaPrP90-232 exhibited a less rigid but still strong hydrogen bonding pattern as indicated by the β-sheet specific difference band at 1624 cmâ1. The denaturation/aggregation temperature of SHaPrP90-232 was consistently determined using the β-sheet specific difference band observed in the H2O or in the D2O experiments. Further, the spectra obtained for the critical oligomers produced in appropriate buffer systems at 25 °C and at 37 °C revealed no significant differences in secondary structure.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Vibrational Spectroscopy - Volume 38, Issues 1â2, 29 July 2005, Pages 39-44
Journal: Vibrational Spectroscopy - Volume 38, Issues 1â2, 29 July 2005, Pages 39-44
نویسندگان
Fabian Sokolowski, Dieter Naumann,