Back in the 90s I did some research on the molecular chaperone GroEL, which at the time didn't even have a crystal structure to its name. It is a great pleasure to see that the accumulation of structural and functional knowledge on this protein has now reached the stage where researchers can assemble snapshots to a movie showing plausible twists and turns that the seen subunits of each ring may carry out during their functional cycle.
The paper from Helen Saibil and colleagues at Birkbeck College, London, appeared in Cell (online) yesterday (D K Clare et al, Cell, 2012, DOI: 10.1016/j.cell.2012.02.047) and I wrote a news item for Chemistry World which has gone live today:
Molecular chaperones caught on film.
PS (23.4.2012): a related paper that just came out in Biophys J. and is freely accessible: Prying Open Single GroES Ring Complexes by Force Reveals Cooperativity across Domains
Akiko Ikeda-Kobayashi, Yukinori Taniguchi, David J. Brockwell, Emanuele Paci and Masaru Kawakami
Biophysical Journal, Volume 102, Issue 8, 1961-1968, 18 April 2012