ADVERTISEMENT
ADVERTISEMENT

Biochemistry/ Structural Biology

K. Braig, Z. Otwinowski, R. Hegde, D.C. Boisvert, A.Joachimiak, A.L. Horwich, P.B. Sigler, "The crystal structure of the bacterial chaperonin GroEL at 2.8 angstroms," Nature, 371:578-86, 1994. (Cited in more than 100 publications as of February 1996) 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 Sigle

Neeraja Sankaran
K. Braig, Z. Otwinowski, R. Hegde, D.C. Boisvert, A.Joachimiak, A.L. Horwich, P.B. Sigler, "The crystal structure of the bacterial chaperonin GroEL at 2.8 angstroms," Nature, 371:578-86, 1994. (Cited in more than 100 publications as of February 1996)

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

Arthur Horwich Paul Sigler
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...

Interested in reading more?

Become a Member of

Receive full access to digital editions of The Scientist, as well as TS Digest, feature stories, more than 35 years of archives, and much more!
Already a member?
ADVERTISEMENT