Preparation and Properties of a 3,4-Dihydroxycinnamic Acid Chromophore Variant of the Photoactive Yellow Protein
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference17 articles.
1. Isolation and characterization of soluble cytochromes, ferredoxins and other chromophoric proteins from the halophilic phototrophic bacterium Ectothiorhodospira halophila
2. Soluble cytochromes and a photoactive yellow protein isolated from the moderately halophilic purple phototrophic bacterium, Rhodospirillum salexigens
3. Occurrence and purification of the photoactive yellow protein of Ectothiorhodospira halophila (PYP) and of immunologically related proteins of Rhodospirillum salexigens and Chromatium salexigens and intracellular localization of PYP
4. The xanthopsins: a new family of eubacterial blue-light photoreceptors.
5. Primary structure of a photoactive yellow protein from the phototrophic bacteriumEctothiorhodospira halophila, with evidence for the mass and the binding site of the chromophore
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1. Structural and spectroscopic characterization of photoactive yellow protein and photoswitchable fluorescent protein constructs containing heavy atoms;Journal of Photochemistry and Photobiology A: Chemistry;2020-10
2. Detection of Incorporation of p-Coumaric Acid into Photoactive Yellow Protein Variants in Vivo;Biochemistry;2019-05-22
3. Origins of the Intermediate Spectral Form in M100 Mutants of Photoactive Yellow Protein;Photochemistry and Photobiology;2015-05-28
4. Influence of a chromophore analogue in the protein cage of a photoactive yellow protein;Photochemical & Photobiological Sciences;2015
5. Optical Control of Protein–Protein Interactions via Blue Light-Induced Domain Swapping;Biochemistry;2014-07-16
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