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Spectral studies on the structure of apoCopC and Cu2+-CopC
The role of cupric in maintaining the structure of CopC

Keywords: apoCopC,CuN 2 -CopC,urea,spectra
二价铜
,CopC,蛋白质结构,构象稳定性,作用,尿素变性

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Abstract:

The CopC protein from pseudomonas syringae pathovar tomato is expressed as one of four proteins encoded by the operon CopABCD that is responsible for copper resistance. And there are one tryptophan (83), one tyrosine (79), and three phenylalanines (35, 43, 99) in apoCopC. The fluorescence peak of apoCopC is located near 320 nm, and the peak shifts toward 353 nm in the presence of 10 mol·L 1 urea with excitation at 280 nm. Using urea as a chemical agent, the conformational stabilities of apoCopC and Cu N 2+ -CopC were monitored by fluorescence spectrum in 20 mmol·L 1 phosphate buffer and 100 mmol·L 1 sodium chloride at pH 6.0. The free energy of stabilization for apoCopC and Cu N 2+ -CopC is 16.29±0.65 kJ·mol 1 and 26.26±0.35 kJ·mol 1, respectively. The distance between the tryptophan residue and the Cu2+ in Cu N 2+ -CopC has been studied by observing F?rster type nonradiative energy transfer. And it is calculated to be 11.6 ?. Supported by the National Natural Science Foundation of China (Grant No. 20371031), and the Natural Science Foundation of Shanxi Province (Grant No. 20031017)

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