The dynamics of single protein molecules is non-equilibrium and self - similar over thirteen decades in time
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The dynamics of single protein molecules is non-equilibrium and self - similar over thirteen decades in time subscribers only.
A persistent challenge in unraveling mechanisms that regulate memory function is how to bridge the gap between inter-molecular
dynamics of single proteins, activity of individual synapses and emerging properties of neuronal circuits.
Not exact matches
A: I'm working on using solid - state defects in diamonds as magnetic field sensors, with the goal
of using them as little nanoscale MRI machines that can study the structure and
dynamics of single biological molecules (e.g.,
proteins).
We demonstrated the technique on 20 different biological processes spanning four orders
of magnitude in space and time, including the binding kinetics
of single Sox2 transcription factor molecules, 3D superresolution photoactivated localization microscopy
of nuclear lamins, dynamic organelle rearrangements and 3D tracking
of microtubule plus ends during mitosis, neutrophil motility in a collagen mesh, and subcellular
protein localization and
dynamics during embryogenesis in Caenorhabditis elegans and Drosophila melanogaster.
We will use high and super-resolution fluorescence microscopy like total internal reflection fluorescence microscopy (TIRFM) and fluorescence photo - activation localization microscopy (FPALM) to visualize and track the spatio - temporal
dynamics of tethering and SNARE
proteins in live and fixed cells with
single molecule resolution.
All
of them are shown to be affected by a
single protein in their picosecond hydrogen bond
dynamics