کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10536953 | 962647 | 2010 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A broad glass transition in hydrated proteins
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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 performed Raman and Brillouin scattering measurements to estimate glass transition temperature, Tg, of hydrated protein. The measurements reveal very broad glass transition in hydrated lysozyme with approximate Tg â¼Â 180 ± 15 K. This result agrees with a broad range of Tg â¼Â 160-200 K reported in literature for hydrated globular proteins and stresses the difference between behavior of hydrated biomolecules and simple glass-forming systems. Moreover, the main structural relaxation of the hydrated protein system that freezes at Tg â¼Â 180 K remains unknown. We emphasize the difference between the “dynamic transition”, known as a sharp rise in mean-squared atomic displacement at temperatures around TD â¼Â 200-230 K, and the glass transition. They have different physical origin and should not be confused.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1804, Issue 1, January 2010, Pages 15-19
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1804, Issue 1, January 2010, Pages 15-19
نویسندگان
S. Khodadadi, A. Malkovskiy, A. Kisliuk, A.P. Sokolov,