کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9743531 | 1491193 | 2005 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Application of multivariate curve resolution to the temperature-induced unfolding of α-chymotrypsin
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
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چکیده انگلیسی
The application of the chemometric method multivariate curve resolution-alternating least-squares (MCR-ALS) to the spectroscopic measurements allowed for the recovery of the concentration profiles and spectra of three different protein conformations, one of them not obtainable experimentally. Joining the resolved information about the evolution of the tertiary structure and the results coming from methods devoted to the elucidation of the protein secondary structure, the three protein conformations can be characterised as: a native conformation, with both secondary and tertiary structure organized as in the natural active protein; a second conformation, with a modified secondary structure richer in β-sheet and a native-like tertiary structure, and a third conformation, with a secondary structure very similar to the second conformation and with the tertiary structure unfolded.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Analytica Chimica Acta - Volume 544, Issues 1â2, 15 July 2005, Pages 159-166
Journal: Analytica Chimica Acta - Volume 544, Issues 1â2, 15 July 2005, Pages 159-166
نویسندگان
Anna Borges, Romà Tauler, Anna de Juan,