Jianzhong Wen

TL;DR: Evidence that quantum coherence survives in FMO at physiological temperature for at least 300 fs, long enough to impact biological energy transport is presented, proving that the wave-like energy transfer process discovered at 77 K is directly relevant to biological function.

TL;DR: Fam20C appears to be the Golgi casein kinase that phosphorylates secretory pathway proteins within S-x-E motifs, and is thus a protein kinase dedicated to the phosphorylation of extracellular proteins.

TL;DR: A new analysis of the previously published X-ray data for the Chlorobaculum tepidum FMO shows the presence of a Bacteriochlorophyll-a molecule in an equivalent location but with a chemical attachment from only one side, which is shown to be predictive of the spectral type of the FMO.

TL;DR: Fam20C is established as the major secretory pathway protein kinase and serve as a foundation for new areas of investigation into the role of secreted protein phosphorylation in human biology and disease.

TL;DR: A mass spectrometry-based method that probes solvent-exposed surfaces of the FMO by labeling solvent-Exposed aspartic and glutamic acid residues reveals the orientation and provides direct experimental evidence to confirm the overall architecture of the photosystem from Chlorobaculum tepidum and give information on the packing of theFMO protein in its native environment.