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A study of the denaturation of human C-reactive protein in the presence of calcium ions and glycero-phosphorylcholine by Richard J. Heaton; John G. Raynes; David S. Johnston is a Materials Science article available to read on EtoBox.

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Differential scanning calorimetry, fourier transform infrared spectroscopy and surface plasmon resonance spectrometry have been used to study the thermal properties of C-reactive protein in its ligand-bound and ligand-free forms. Clear denaturation endotherms were detected during calorimeter heating scans. Upon binding either or both its ligands, Ca 2 and glycero-phosphorylcholine, the denaturation temperature of the protein and the enthalpy change on denaturation were increased. Marked changes in the infrared spectrum of the protein were seen when it was heated. The main absorption peaks in the spectrum, at 1651 and 1643 cm À1 were replaced by a single peak at 1628 cm À1 . There was an isosbestic point at 1630 cm À1 . Comparison with the calorimetric data indicated that the changes in spectra were caused by protein denaturation. The spectra, like the calorimetric data, showed that the presence of glycero-phosphorylcholine raised the denaturation temperature of the protein. However, the presence of calcium ions had little effect on the spectra. This suggests that unlike glycero-phosphorylcholine, calcium binds to C-reactive protein in such a way that hydrogen bonding in the polypep

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Author

Richard J. Heaton; John G. Raynes; David S. Johnston

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0040-6031)

Published

1999

Language

EN

Field

Materials Science (Physical Sciences)