T.R. Sosnick, L. Mayne, R. Hiller, S.W. Englander, "The barriers in protein folding," Nature Structural Biology 1:149-156, 1994. (Cited in approximately 40 publications through July 1995)

Comments by S. Walter Englander, University of Pennsylvania Medical Center

"The protein folding problem--the way in which unfolded proteins manage to reach their native, three-dimensional, functional form--has become a central focus for many scientists," declares Walter Englander, a professor of biochemistry and biophysics at the University of Pennsylvania Medical Center. For instance, he elaborates, "protein chemists care about it for pure science; cell biologists are interested in it with respect to cell stress proteins called chaperones; and it is a big-money issue for the protein designers and pharmacological chemists who want to clone proteins in unusual environments or design new proteins.

SLOW TRACK, FAST TRACK: From left, Tobin Sosnick, Wlater Englander, and Leland Mayne have proposed that the rate-limiting step in protein folding...

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