More subtleties in protein structure and function

Almost three years ago I posted about the controversy concerning whether the photoactive yellow protein has low-barrier hydrogen bonds [for these the energy barrier for proton transfer is comparable to the zero-point energy]. I highlighted just how difficult it is going to be, both experimentally and theoretically to definitively resolve the issue, just as for an enzyme I recently discussed.
A key issue concerns how to interpret large proton NMR chemical shifts.

Two recent papers weigh in on the issue

The Low Barrier Hydrogen Bond in the Photoactive Yellow Protein: A Vacuum Artifact Absent in the Crystal and Solution 
Timo Graen, Ludger Inhester, Maike Clemens, Helmut Grubmüller, and Gerrit Groenhof

A Dynamic Equilibrium of Three Hydrogen-Bond Conformers Explains the NMR Spectrum of the Active Site of Photoactive Yellow Protein 
Phillip Johannes Taenzler, Keyarash Sadeghian, and Christian Ochsenfeld

I think the caveats I have offered before need to kept in mind.
As with understanding the active sites of most proteins the problem is that we don't have very direct experimental probes, but have to use indirect probes which produce experimental results that require significant modelling and interpretation.

I thank Steve Boxer for bringing one of these papers to my attention.