A QUANTITATIVE SECONDARY STRUCTURE-ANALYSIS OF THE 33-KDA EXTRINSIC POLYPEPTIDE OF PHOTOSYSTEM-II BY FTIR SPECTROSCOPY

被引：109
作者：
AHMED, A [1 ]
TAJMIRRIAHI, HA [1 ]
CARPENTIER, R [1 ]
机构：
[1] UNIV QUEBEC,CTR RECH PHOTOBIOPHYS,TROIS RIVIERES,PQ G9A 5H7,CANADA
来源：
FEBS LETTERS | 1995年 / 363卷 / 1-2期
关键词：
33 KDA EXTRINSIC; PROTEIN; CONFORMATION; PSII REACTION CENTER; FTIR SPECTROSCOPY;
D O I：
10.1016/0014-5793(95)00282-E
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
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 beta-sheet conformation (36%) with 27% alpha-helix, 24% turn, and 13% beta-antiparallel structures.
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页码：65 / 68
页数：4
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