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EosFP, a fluorescent marker protein with UV-inducible green-to-red fluorescence conversion.
A gene encoding a fluorescent protein from the stony coral Lobophyllia hemprichii has been cloned in Escherichia coli and characterized by biochemical and biophysical methods and is found to be tetrameric, with strong Forster resonance coupling among the individual fluorophores. Expand
Neuroglobin, nitric oxide, and oxygen: functional pathways and conformational changes.
Based on the ligand-linked conformational changes discovered by crystallography, the pathways of the reactions with O2 and NO provide a framework that may account for the involvement of Ngb in controlling the activation of a protective signaling mechanism. Expand
Differential uptake of functionalized polystyrene nanoparticles by human macrophages and a monocytic cell line.
The data show that the amount of internalized nanoparticles, the uptake kinetics, and its mechanism may differ considerably between primary cells and a related tumor cell line, whether differentiated or not, and that particle uptake by these cells is critically dependent on particle opsonization by serum proteins. Expand
Engineered nanoparticles interacting with cells: size matters
Common techniques to characterize NP size are summarized, recent work on the impact of NP size on active and passive cellular internalization and intracellular localization are highlighted and Cytotoxic effects are discussed. Expand
Structural basis for photo-induced protein cleavage and green-to-red conversion of fluorescent protein EosFP.
X-ray structures of the green and red forms of WT EosFP reveal that formation of the red chromophore is associated with cleavage of the peptide backbone, with surprisingly little change elsewhere in the structure, and provide insights into the mechanism that generates this interesting posttranslational polypeptide modification. Expand
Ligand binding and conformational motions in myoglobin
It is shown that below 180 K photodissociated ligands migrate to specific sites within an internal cavity—the distal haem pocket— of an essentially immobilized, frozen protein, from where they subsequently rebind by thermally activated barrier crossing. Expand
A quantitative fluorescence study of protein monolayer formation on colloidal nanoparticles.
It is now known that nanoparticles, when exposed to biological fluid, become coated with proteins and other biomolecules to form a 'protein corona'. Recent systematic studies have identified variousExpand
Structural basis of enhanced photoconversion yield in green fluorescent protein-like protein Dendra2.
The structure, which is very similar to those reported for the closely related proteins EosFP and Kaede, revealed a local structural change involving mainly Arg66 and a water molecule W4, which are part of a charged and hydrogen-bonded cluster of amino acids and water molecules next to the chromophore. Expand
Ultra-small fluorescent metal nanoclusters: Synthesis and biological applications
Abstract Recent advances in nanotechnology have given rise to a new class of fluorescent labels, fluorescent metal nanoclusters, e.g., Au and Ag. These nanoclusters are of significant interestExpand
A far-red fluorescent protein with fast maturation and reduced oligomerization tendency from Entacmaea quadricolor (Anthozoa, Actinaria)
The biochemical and biophysical characterization of a red fluorescent protein from the sea anemone Entacmaea quadricolor cloned in Escherichia coli found that it shows the most red-shifted emission and the largest Stokes shift of all nonmodified proteins in the green fluorescent protein family. Expand