Structure and function of native and refolded peridinin-chlorophyll-proteins from dinoflagellates.

No abstract is available for this paper.

• Publication year

  2010

• Venue

  European Journal of Cell Biology

• Publication date

  2010-12-01

• Fields of study

  Biology, Medicine, Chemistry, Environmental Science

• Identifiers
  DOI 10.1016/j.ejcb.2010.08.004PMID 20846743
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• X‐ray structures of the peridinin–chlorophyll‐protein reconstituted with different chlorophylls

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  2009cited by this paper
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  2009cited by this paper
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  2009cited by this paper
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  2008cited by this paper
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  2008cited by this paper
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  2008cited by this paper
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  2008cited by this paper
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  2007cited by this paper
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  2007cited by this paper
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• Energy transfer in reconstituted peridinin-chlorophyll-protein complexes: ensemble and single-molecule spectroscopy studies.

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• Post-crystallization treatments for improving diffraction quality of protein crystals.

  2005cited by this paper
• Tuning Energy Transfer in the Peridinin–chlorophyll Complex by Reconstitution with Different Chlorophylls

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• Reconstitution of the Peridinin–chlorophyll a Protein (PCP): Evidence for Functional Flexibility in Chlorophyll Binding

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• Light Regulation of Peridinin-Chlorophyll a-Protein (PCP) Complexes in the Dinoflagellate, Glenodinium sp. : Use of Anti-Pcp Antibodies to Detect Pcp Gene Products in Cells Grown in Different Light Conditions.

  1988cited by this paper
• Conceptual Structures

  1984cited by this paper
• Molecular topology of the photosynthetic light-harvesting pigment complex, peridinin-chlorophyll a-protein, from marine dinoflagellates.

  1976cited by this paper

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