Results 241 to 250 of about 2,532,057 (298)
Kinetic isotope effect reveals rate-limiting step in green-to-red photoconvertible fluorescent proteins. [PDF]
Breen B, Whitelegge JP, Wachter RM.
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Bright lights, big synapses: fluorescent proteins let neurons shine. [PDF]
Ackley BD.
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Fusing fluorescent proteins and ferritin for protein cage based lighting devices.
Sanz-Velasco A +7 more
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Engineering highly stable variants of Corynactis californica green fluorescent proteins. [PDF]
Hung LW +3 more
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Fluorescence Lifetime of Fluorescent Proteins
Jung G, Brockhinke A, Gensch T, Hötzer B, Schwedler S, Veettil SK. Fluorescence lifetime of fluorescent proteins. In: Jung G, ed. Fluorescent Proteins I. From Understanding to Design. Springer Series on Fluorescence 11.
Jung, Gregor +6 more
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The Role of the Protein Matrix in Green Fluorescent Protein Fluorescence
Photochemistry and Photobiology, 2006ABSTRACTIn the ground state of the highly conjugated green fluorescent protein (GFP), the chromophore should be planar. However, numerous crystal structures of GFP and GFP‐like proteins have been reported with slightly twisted chromophores. We have previously shown that the protein cavity surrounding the chromophore in wild‐type GFP is not ...
Scott L, Maddalo, Marc, Zimmer
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Fluorescent proteins for single‐molecule fluorescence applications
Journal of Biophotonics, 2008AbstractWe present single‐molecule fluorescence data of fluorescent proteins GFP, YFP, DsRed, and mCherry, a new derivative of DsRed. Ensemble and single‐molecule fluorescence experiments proved mCherry as an ideally suited fluorophore for single‐molecule applications, demonstrated by high photostability and rare fluorescence‐intensity fluctuations ...
Seefeldt, Britta +6 more
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Optimization of Fluorescent Proteins
2013Nowadays, fluorescent protein (FP) variants have been engineered to fluoresce in all different colors; to display photoswitchable, or photochromic, behavior; or to show yet other beneficial properties that enable or enhance a still growing set of new fluorescence spectroscopy and microcopy techniques.
Bindels, D.S. +5 more
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TYROSINE FLUORESCENCE IN PROTEINS
Annals of the New York Academy of Sciences, 1969SummaryThe problem of observing tyrosine emission in proteins containing tryptophan is related to both the absorption and emission properties of these two amino acids. First, the absorption of tryptophan is several times larger than tyrosine at all wavelengths.
H, Edelhoch, R L, Perlman, M, Wilchek
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