منابع مشابه
Polarized fluorescence resonance energy transfer microscopy.
Current methods for fluorescence resonance energy transfer (FRET) microscopy of living cells involve taking a series of images with alternating excitation colors in separate camera exposures. Here we present a new FRET method based on polarization that requires only one camera exposure and thereby offers the possibility for better time resolution of dynamic associations among subcellular compon...
متن کاملFluorescence resonance energy transfer scanning near-field optical microscopy.
The method of fluorescence resonance energy transfer scanning near-field optical microscopy (FRET SNOM) consists in the separation of a FRET pair between an SNOM tip and a sample. The donor (or acceptor) centre is located at the tip apex and scanned in the vicinity of a sample while acceptor fluorescence (or donor-fluorescence quenching) is detected. It is shown that the spatial resolution for ...
متن کامل[13] Fluorescence Resonance Energy Transfer
of the extent of binding. This effect (known informally as "Chip dip") is illustrated in Figs. 6 and 7 which concern the ethidium bromide/tRNA system. 41 In this case the free ethidium bromide has a lifetime of 1.86 nsec and a rotational relaxation time of 0.54 nsec. On binding the PhetRNA Phe the lifetime increases to 26 nsec and the rotational relaxation increases to 136 nsec. A single rotati...
متن کاملNicotinic Channels Measured with Fluorescence Resonance Energy Transfer and Total Internal Reflection Fluorescence Microscopy
Structurally distinct nicotinic and P2X channels interact functionally, such that coactivation results in cross-inhibition of one or both channel types. It is hypothesized, but not yet proven, that nicotinic and P2X channels interact at the plasma membrane. Here, we show that plasma membrane 4 2 nicotinic and P2X2 channels form a molecular scale partnership and also influence each other when co...
متن کاملSingle-molecule fluorescence resonance energy transfer.
Fluorescent resonance energy transfer (FRET) is a powerful technique for studying conformational distribution and dynamics of biological molecules. Some conformational changes are difficult to synchronize or too rare to detect using ensemble FRET. FRET, detected at the single-molecule level, opens up new opportunities to probe the detailed kinetics of structural changes without the need for syn...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2004
ISSN: 0006-3495
DOI: 10.1529/biophysj.103.036194