Picosecond Protein Watching

There are a good number of pico-second resolved X-ray crystallography papers published. Schotte, the author here, published her first in 2003 on Myoglobin. Many others have used this since the early 2000s. Other protein watching techniques such as NMR have been exploited for small time resolution, as well.

The frontier to be talked about is single molecule resolution. Equilibrium measurements, like X-ray crystallography, are still incapable of picking up states of the protein with very low populations, which are often relevant to conformational change.

It can be a bit of misnomer, as well. Time resolution of often means using a singular value decomposition to pull out populated states from the data. As a result, the pictures isn't exactly time linear.

interesting. my education is as a biochemist, and my interest was in protein dynamics. i knew the x-ray guys were trying to get to this, and it was only a matter of time before they could image and compute fast enough. i had expected the NMR guys to get there first, however.

This is going to be incredibly big for the protein structure predictors as well. Most of the best models incorporate bond-breaking and conformational switching moves as described in the function of this protein, but the vast combinatorial possibilities make it hard to resolve what the folding paths are to the global minimum and which are "unnatural" and leave you sitting in a local minima. Tweaking their models with real-world input from this type of imaging and more sophisticated statistics about the frequency of moves will work wonders for their automated efforts.

Won't the protein absorbing x-rays affect its reaction?