کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5375797 | 1504304 | 2008 | 12 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Fluorescence, anisotropy and docking studies of proteins through excited state intramolecular proton transfer probe molecules
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی تئوریک و عملی
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چکیده انگلیسی
The enhanced fluorescence and anisotropy of the ESIPT emission of 3-hydroxy-2-naphthoic acid (3HNA) in the complexes of 3HNA with bovine serum albumin (BSA) and human serum albumin (HSA) showed the formation of 1:1 complex [binding constant = 5.3 Ã 105 Mâ1 for BSA and = 2.2 Ã 105 Mâ1 for HSA]. The ESIPT emission of the probe in non-polar, polar protic, polar aprotic and mixed solvents indicate that the position and the quantum yield of the emission are governed by the intermolecular hydrogen bonding ability and the polarity/polarizability of the solvents. Rotational correlation time of 3HNA (2.4 ns and 5.2 ns in BSA and HSA, respectively) obtained from the time resolved anisotropy decay of the ESIPT emission suggests motional restriction of the probe. Docking studies reveal H-bonding of some residues with the probe and loss of accessible surface area of several residues located near binding site.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Chemical Physics - Volume 354, Issues 1â3, 10 December 2008, Pages 162-173
Journal: Chemical Physics - Volume 354, Issues 1â3, 10 December 2008, Pages 162-173
نویسندگان
Shyam Sundar Maity, Subhodip Samanta, Pinki Saha Sardar, Anirban Pal, Swagata Dasgupta, Sanjib Ghosh,