The intrinsic fluorescence of apo-obelin and apo-aequorin and use of its quenching to characterize coelenterazine binding.
about
Red-Shifted Aequorin Variants Incorporating Non-Canonical Amino Acids: Applications in In Vivo ImagingThe light-sensitive photoprotein berovin from the bioluminescent ctenophore Beroe abyssicola: a novel type of Ca(2+) -regulated photoprotein.Dynamic chirality determines critical roles for bioluminescence in symplectin-dehydrocoelenterazine system.Ligand binding and conformational states of the photoprotein obelin.Transient-state kinetic analysis of complex formation between photoprotein clytin and GFP from jellyfish Clytia gregaria.Unanimous Model for Describing the Fast Bioluminescence Kinetics of Ca2+ -regulated Photoproteins of Different Organisms.Tyr72 and Tyr80 are Involved in the Formation of an Active Site of a Luciferase of Copepod Metridia longa.Hydrogen-bond networks between the C-terminus and Arg from the first α-helix stabilize photoprotein molecules.
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P2860
The intrinsic fluorescence of apo-obelin and apo-aequorin and use of its quenching to characterize coelenterazine binding.
description
2009 nî lūn-bûn
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2009年の論文
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2009年学术文章
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name
The intrinsic fluorescence of ...... terize coelenterazine binding.
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The intrinsic fluorescence of ...... terize coelenterazine binding.
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type
label
The intrinsic fluorescence of ...... terize coelenterazine binding.
@en
The intrinsic fluorescence of ...... terize coelenterazine binding.
@nl
prefLabel
The intrinsic fluorescence of ...... terize coelenterazine binding.
@en
The intrinsic fluorescence of ...... terize coelenterazine binding.
@nl
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The intrinsic fluorescence of ...... cterize coelenterazine binding
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Adrie H Westphal
Antonie J W G Visser
Svetlana V Markova
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10.1016/J.FEBSLET.2009.04.043
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2009-05-06T00:00:00Z