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Updated: Jan 29, 2026

Pull-down of Calmodulin-binding Proteins
Published on: January 23, 2012
Coordination to Divalent Cations by Calcium-Binding Proteins
Masayuki Nara1, Hisayuki Morii2, Masaru Tanokura3
1Department of Chemistry, College of Liberal Arts and Sciences, Tokyo Medical and Dental University, Chiba, Japan. nara.las@tmd.ac.jp.
Abstract:
Fourier-transform infrared spectroscopy (FTIR) is a powerful tool for examining the metal coordination of the side chain COO- groups of Glu and Asp on Ca2+-binding proteins in solution. The behavior of COO- symmetric stretch can be investigated by using protein samples in H2O solution. However, it is difficult to obtain information about the behavior of the COO- antisymmetric stretch in H2O solution, because the COO- antisymmetric stretching band overlaps with the amide II band. Therefore, to obtain reliable infrared spectra in the region of COO- antisymmetric stretch, exchangeable protons in the protein should be completely deuterated by incubating the apoprotein dissolved in D2O under mild heating conditions.
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