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- W2141098637 abstract "The secondary structures of human C-reactive protein (CRP) and serum amyloid P component (SAP) in D,Obased solutions in the presence or absence of calcium, magnesium, and phosphorylcholine have been investigated using Fourier transform infrared spectroscopy. Quantitative analysis provided estimations of about 50% @-sheet, 12% a-helix, 24% @-turn, and 14% unordered structure for CRP and about 54% @-sheet, 12% a-helix, 25% @-turn, and 9% unordered structure for SAP. With both proteins significant calcium-dependent changes were observed in conformation-sensitive amide I regions assigned to each type of structure. The CRP spectrum was also af€ected by magnesium, but the changes differed from those induced by calcium. The SAP spectrum was not affected by magnesium. Phosphorylcholine in the presence of calcium also affected the spectrum of CRP but not the spectrum of SAP. Our present study provides the first direct comparison of the secondary structures of the pentraxins human CRP and SAP and hamster female protein (Dong, A., Caughey, B., Caughey, W. S., Bhat, K. S., and Coe, J. E. (1992) Biochemistry 32, 9364-9370). These findings suggest that the three pentraxins have similar secondary structure compositions and calcium-dependent conformational" @default.
- W2141098637 created "2016-06-24" @default.
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- W2141098637 date "1994-03-01" @default.
- W2141098637 modified "2023-09-27" @default.
- W2141098637 title "Effects of calcium, magnesium, and phosphorylcholine on secondary structures of human C-reactive protein and serum amyloid P component observed by infrared spectroscopy." @default.
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- W2141098637 doi "https://doi.org/10.1016/s0021-9258(17)37389-1" @default.
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