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.
KNOWING WHEN TO FOLD: Judith Frydman and F. Ultrich Hartl tested a hypothesis concerning protein folding.
Using the folding of the protein luciferase from fireflies as a model, the researchers "attempted to answer two main questions: first, whether molecular chaperones were involved in protein folding during translation; and second, which chaperone systems participated in ...
