W.A. Fenton, Y. Kashi, K. Furtak, A. Horwich, "Residues in chaperonin GroEL required for polypeptide binding and release," Nature, 371:614-9, 1994. (Cited in more than 60 publications as of February 1996)
Comments by Arthur Horwich and Paul Sigler, Yale University School of Medicine and Howard Hughes Medical Institute
A 'Mystical Experience': Teams led by Yale researchers Arthur Horwich, left, and Paul Sigler solved the structure of the bacterial chaperonin GroEL.
Early electron microscopy (em) studies detected the large central channel in GroEL and showed that proteins that were not folded could bind inside this channel. Now, through the collaboration of two Yale University research labs, the atomic-level details of GroEL structure and functional implications have been elucidated.
"The production of decent, well-diffracting crystals was a major problem," comments Arthur Horwich, a professor of genetics at Yale University School of Medicine and an associate investigator of the Howard Hughes Medical Institute. ...
