FEBS Letters | |
A quantitative secondary structure analysis of the 33 kDa extrinsic polypeptide of photosystem II by FTIR spectroscopy | |
Carpentier, R.1  Ahmed, A.1  Tajmir-Riahi, H.A.1  | |
[1] Centre de recherche en photobiophysique, Université du Québec a Trois-Rivières, CP. 500, Trois-Rivières, Québec, G9A 5H7, Canada | |
关键词: 33 kDa extrinsic; Protein; Conformation; PSII reaction center; FTIR spectroscopy; PSII; photosystem II; SDS; sodium dodecyl sulfate; CD; circular dichroism; FTIR; Fourier transform infrared; | |
DOI : 10.1016/0014-5793(95)00282-E | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
In chloroplast photosystem II, the extrinsic polypeptide of 33 kDa is involved in the stabilization the Mn cluster in charge of water splitting and in the fulfillment of the Ca2+-cofactor requirement for oxygen evolution. The conformational analysis of the purified 33 kDa extrinsic polypeptide was carried out using FTIR spectroscopy with its self-deconvolution and second derivative resolution enhancement as well as curve-fitting procedures. The FTIR spectroscopic results showed that the isolated polypeptide is characterized by a major proportion β-sheet conformation (36%) with 27% α-helix, 24% turn, and 13% β-antiparallel structures.
【 授权许可】
Unknown
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Files | Size | Format | View |
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RO201912020300950ZK.pdf | 556KB | download |