کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10766852 | 1050679 | 2008 | 15 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Infrared spectroscopic study of the metal-coordination structures of calcium-binding proteins
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
Carboxylate (COOâ) groups can coordinate to metal ions in of the following four modes: 'unidentate', 'bidentate', 'bridging' and 'pseudo-bridging' modes. COOâ stretching frequencies provide information about the coordination modes of COOâ groups to metal ions. We review the Fourier-transform infrared spectroscopy (FTIR) of side-chain COOâ groups of Ca2+-binding proteins: pike parvalbumin pI 4.10, bovine calmodulin and Akazara scallop troponin C. FTIR spectroscopy of Akazara scallop troponin C has demonstrated that the coordination structure of Mg2+ is distinctly different from that of Ca2+ in the Ca2+-binding site. The assignments of the COOâ antisymmetric stretch have been ensured on the basis of the spectra of calcium-binding peptide analogues. The downshift of the COOâ antisymmetric stretching mode from 1565 cm-1 to 1555-1540 cmâ1 upon Ca2+ binding is a commonly observed feature of FTIR spectra for EF-hand proteins.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 369, Issue 1, 25 April 2008, Pages 225-239
Journal: Biochemical and Biophysical Research Communications - Volume 369, Issue 1, 25 April 2008, Pages 225-239
نویسندگان
Masayuki Nara, Masaru Tanokura,