Photobleaching Pathways in Single-Molecule FRET Experiments
نویسندگان
چکیده
منابع مشابه
Single-molecule switchable FRET
Two-photon microscopy offers unique advantages for excitation of channelrhodopsin-2 (ChR2)-expressing neurons, but previous attempts had limitations in terms of the axial and temporal resolution. Emiliani and colleagues now use a scanless approach that combines generalized phase contrast and temporal focusing to shape two-photon excitation patterns and trigger single action potentials or trains...
متن کاملSingle-molecule three-color FRET.
Fluorescence resonance energy transfer (FRET) measured at the single-molecule level can reveal conformational changes of biomolecules and intermolecular interactions in physiologically relevant conditions. Thus far single-molecule FRET has been measured only between two fluorophores. However, for many complex systems, the ability to observe changes in more than one distance is desired and FRET ...
متن کاملInferring subunit stoichiometry from single molecule photobleaching
Single molecule photobleaching is a powerful tool for determining the stoichiometry of protein complexes. By attaching fluorophores to proteins of interest, the number of associated subunits in a complex can be deduced by imaging single molecules and counting fluorophore photobleaching steps. Because some bleaching steps might be unobserved, the ensemble of steps will be binomially distributed....
متن کاملSingle-molecule high-resolution imaging with photobleaching.
Conventional light microscopy is limited in its resolving power by the Rayleigh limit to length scales on the order of 200 nm. On the other hand, spectroscopic techniques such as fluorescence resonance energy transfer cannot be used to measure distances >10 nm, leaving a "gap" in the ability of optical techniques to measure distances on the 10- to 100-nm scale. We have previously demonstrated t...
متن کاملBOBA FRET: Bootstrap-Based Analysis of Single-Molecule FRET Data
Time-binned single-molecule Förster resonance energy transfer (smFRET) experiments with surface-tethered nucleic acids or proteins permit to follow folding and catalysis of single molecules in real-time. Due to the intrinsically low signal-to-noise ratio (SNR) in smFRET time traces, research over the past years has focused on the development of new methods to extract discrete states (conformati...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of the American Chemical Society
سال: 2007
ISSN: 0002-7863,1520-5126
DOI: 10.1021/ja068002s