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

被引：108

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.

引用

页码：65 / 68

页数：4

共 34 条

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