Bilin attachment sites in the alpha and beta subunits of B-phycoerythrin. Structural studies on a doubly peptide-linked phycoerythrobilin.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference14 articles.
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3. The quaternary structure of a unique phycobiliprotein: B-phycoerythrin from Porphyridium cruentum
4. Bilin attachment sites in the alpha and beta subunits of B-phycoerythrin. Amino acid sequence studies.
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1. Direct differentiation of A-ring single attachmentversusA- and D-ring double attachment of phycoerythrobilin chromophores to phycobiliproteins using MALDI mass spectrometry;Journal of Mass Spectrometry;2013-01-29
2. Nonenzymatic bilin addition to the alpha subunit of an apophycoerythrin.;Journal of Biological Chemistry;1994-11
3. Phycobilisome and Phycobiliprotein Structures;The Molecular Biology of Cyanobacteria;1994
4. Organization, expression and nucleotide sequence of the operon encoding R-phycoerythrin ? and ? subunits from the red alga Polysiphonia boldii;Plant Molecular Biology;1993-01
5. Isolation, crystallization, crystal structure analysis and refinement of B-phycoerythrin from the red alga Porphyridium sordidum at 2·2 Å resolution;Journal of Molecular Biology;1992-12
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