کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1408269 | 1501913 | 2006 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Unfolding of apomyoglobin studied with two-dimensional correlations of tryptophan, 8-anilino-1-naphthalenesulfonate, and pyrene fluorescence
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آلی
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چکیده انگلیسی
Acid-induced unfolding of horse apomyoglobin is studied with fluorescence of tryptophan residues and extrinsic probes 8-anilino-1-naphthalenesulfonate (ANS) and pyrene. Two-dimensional statistical correlation coefficient analysis of tryptophan, ANS and pyrene fluorescence reveals that apomyoglobin unfolds in two steps via a folding intermediate. Both tryptophan and ANS fluorescence show microenvironment-sensitive emission maximum and fluorescence intensity. Hetero-spectral 2D correlation analysis reveals that the “red” tryptophan fluorescence correlates with the “red” ANS fluorescence, and the “blue” correlates with the “blue” in the acid-induced unfolding process. Correlation curves are established between the hydrophobicity of the probe-binding site(s) as disclosed by ANS and pyrene fluorescence and the folding extent of apomyoglobin as indicated by tryptophan fluorescence. Two anion-induced refolding intermediates of apomyoglobin: Clâ-induced A-1, and trichloroacetate (TCA)-induced I-2 do not follow the correlation trajectory in the acid-induced unfolding. This suggests that the two anion-induced intermediates do not belong to the low-salt acid-unfolding pathway of apomyoglobin.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Structure - Volume 799, Issues 1â3, 6 November 2006, Pages 177-187
Journal: Journal of Molecular Structure - Volume 799, Issues 1â3, 6 November 2006, Pages 177-187
نویسندگان
Gufeng Wang, M. Lei Geng,