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.
This pair of papers describes the three-dimensional structure of the bacterial chaperonin GroEL, and relates the structural features to the function of GroEL in facilitating protein folding. GroEL is a large, cylindrical protein complex with central channels. These channels...