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Titlebook: Antennas and Reaction Centers of Photosynthetic Bacteria; Structure, Interacti Maria Elisabeth Michel-Beyerle Conference proceedings 1985 S

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期刊全称Antennas and Reaction Centers of Photosynthetic Bacteria
期刊简称Structure, Interacti
影响因子2023Maria Elisabeth Michel-Beyerle
视频video
学科分类Springer Series in Chemical Physics
图书封面Titlebook: Antennas and Reaction Centers of Photosynthetic Bacteria; Structure, Interacti Maria Elisabeth Michel-Beyerle Conference proceedings 1985 S
影响因子The workshop on "Antennas and Reaction Centers of Photosynthetic Bac­ teria" was held at Feldafing, Bavaria (F. R. G. )‘ March 23-25, 1985. This workshop focussed on primary processes with emphasis on structure, inter­ actions and dynamics. It assessed structural, spectroscopic and dynamic data which have accumulated recently, providing an overview of the mech­ anism of the acquisition, storage and useful disposal of energy in bacterial photosynthesis. This volume is a record of the invited papers presented at the workshop. The material was organized into five sections: I. Antennas: Structure and Energy Transfer II. Reaction Centers: Structure and Interactions III. Electron Transfer: Theory and Model Systems IV. Reaction Cen,ters: Structure and Dynamics V. Model Systems on Function of Antennas and Reaction Centers I would like to express my gratitude to all the participants in the work­ shop for their contributions, and to the authors for the timely preparation of their manuscripts. I am indebted to the members of the organizing committee, Professors Sighart F. Fischer and Hugo Scheer for their most valuable assistance and advice. The workshop would not have been so successful with
Pindex Conference proceedings 1985
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Fluorescence Behaviour of Crystallized C-Phycocyanin (Trimer) from ,rgy-transfer between the phycocyanobilin chromophors, this biliprotein has the advantage that by now much is known about the structure of both the chromophor [1] and the protein [2, 3]. It was furthermore established that the fluorescence properties depend sensitively on temperature and the state of
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Bacteriochlorophyll ,- and ,-Protein Complexes from Chlorosomes of Green Sulfur Bacteria Compared wisting pigment [1]. In both groups all of the BChl . is located in chlorosomes, oblong bodies appressed to the inner surface of the cytoplasmic membrane as shown in Fig. 1. Inside the chlorosome are proteinaceous structures called rod elements which are thought to be made up of BChl .—binding protein
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Reverse-Phase High-Performance Liquid Chromatography of Antenna Pigment- and Chlorosomal Proteins oflation and separation of low molecular weight proteins (Mr 5000) and polypeptide fragments generated by enzymic or chemical cleavage of proteins. (1, 2). The distinct advantages of RP-HPLC, speed, sensitivity, reproducibility and resolution, have contributed to great advances in protein structure an
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