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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 Ca-binding proteins in solution. The behavior of COO symmetric stretch can be investigated by using protein samples in HO solution. However, it is difficult to obtain information about the behavior of the COO antisymmetric stretch in HO 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 DO under mild heating conditions.
This article was published in the following journal.
Name: Methods in molecular biology (Clifton, N.J.)
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A family of intracellular calcium-sensing proteins found predominately in NEURONS and PHOTORECEPTOR CELLS. They contain EF HAND MOTIFS and undergo conformational changes upon calcium-binding. Neuronal calcium-sensor proteins interact with other regulatory proteins to mediate physiological responses to a change in intracellular calcium concentration.
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Proteins to which calcium ions are bound. They can act as transport proteins, regulator proteins, or activator proteins. They typically contain EF HAND MOTIFS.
Calcium-binding proteins that are found in DISTAL KIDNEY TUBULES, INTESTINES, BRAIN, and other tissues where they bind, buffer and transport cytoplasmic calcium. Calbindins possess a variable number of EF-HAND MOTIFS which contain calcium-binding sites. Some isoforms are regulated by VITAMIN D.
Neutral or negatively charged ligands bonded to metal cations or neutral atoms. The number of ligand atoms to which the metal center is directly bonded is the metal cation's coordination number, and this number is always greater than the regular valence or oxidation number of the metal. A coordination complex can be negative, neutral, or positively charged.
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