A “Y” shaped protein in the eye


A joint study led by Raquel Lieberman in the School of Chemistry and Biochemistry at GT revealed both the structure and stabilizing mechanisms of the protein myocilin, which is present in the trabecular meshwork of the eye. In particular, simulations demonstrated the role of a key disulfide bond in resisting unfolding. See more about the story here and the paper here.

Workshop success

We just closed out another great Computational Biophysics workshop (the 45th in the series running since 2003!) here in Atlanta. The workshop, sponsored by JC’s former lab in Urbana, covered topics ranging from molecular dynamics to whole cell simulations to even DNA origami! We had about 25 participants from around the southeast (and beyond) spend their week here with us. It was exhausting, but fun, and now we look forward to the next time we will host one again.


The noise is the mechanism

At the NSF iPoLS meeting at Harvard, which JC, Sunny, and Curtis are presenting at, one of the best talks was given by Nigel Goldenfeld (UIUC).

The homochirality of certain biological molecules, especially amino acids in proteins (all L form) and sugars (all D form), has long been a mystery in biology. What processes in early evolution would have led to biological systems using only one form? Hypotheses have included autocatalytic mechanisms as well as even extraterrestrial origins. However, Goldenfeld has recently shown that there’s been a missing ingredient in many of these: the role of noise! Biological systems operate far from equilibrium, and we often find that noise (“stochasticity”) is a beneficial, even critical element, rather than a detrimental background to be minimized. Goldenfeld and colleagues showed that by incorporating two simple principles, self-replication and noise, homochirality can be established.

See a news story here and the original paper here.