J. Frydman, E. Nimmesgern, K. Ohtsuka, F.U. Hartl, "Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones," Nature, 370:111-7, 1994. (Cited in nearly 50 publications through September)

Comments by Judith Frydman and F. Ulrich Hartl, Memorial Sloan-Kettering Cancer Center, New York

This paper describes a series of experiments "analyzing how polypeptide chains fold to their final shapes when being synthesized," according to F. Ulrich Hartl, a member of the cellular biochemistry and biophysics program at New York City-based Memorial Sloan-Kettering Cancer Center, and a Howard Hughes Medical Institute associate investigator there.

Frydman and Hartl KNOWING WHEN TO FOLD: Judith Frydman and F. Ultrich Hartl tested a hypothesis concerning protein folding.

"Although some proteins can fold spontaneously in vitro, it had become increasingly clear that in the cell, certain other components are required to assist in the folding process," remarks Judith Frydman, a postdoctoral fellow in...

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?