Sentences with phrase «protein stoichiometry»

Dr. Lakadamyali states that «at the moment we have to work with imperfect fluorescent proteins and take into account the limitations when quantifying protein stoichiometry, however, now that there is a robust way to characterize photoactivation efficiency, future fluorescent protein engineering work will likely focus on optimizing this parameter for generating fluorescent proteins better suited for molecular counting using super-resolution».

However, despite the «molecular counting» ability that seems intrinsic to the imaging strategy (activating one fluorescent protein at a time should also allow counting how many total fluorescent proteins exist) relating the number of counted fluorescent proteins to actual protein stoichiometry has been difficult.

In a recent study carried out at ICFO, the Institute of Photonic Sciences, the research group of Advanced fluorescence imaging and biophysics, led by Nest Fellow Dr. Melike Lakadamyali was able to quantify the photoactivation efficiency of all the known «ir - reversibly photoswitching fluorescent proteins» and establish a proper detailed reference framework for determining protein stoichiometry.

Not exact matches

The group combines several cutting - edge single molecule imaging techniques to study how protein organization, dynamics and stoichiometry relate to protein function in several fundamental biological processes, such as intracellular transport, autoimmune neurological disorders or stem cell reprogramming.

Therefore, there is a great interest in being able to count proteins and determine their stoichiometry.

To do this, they used a nanotemplate of known stoichiometry (the human Glycine receptor expressed in Xenopus oocytes) and studied several fluorescent proteins to see the percentage of proteins that was photoactivated.

Following a lead from these experiments, we obtained direct evidence for differential stoichiometry among core ribosomal proteins in unperturbed wild - type cells.