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

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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