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 comes from the structural reorganization of the misfolded molecules.
Previously, Englander recounts, "it had been thought that the rate-limiting step occurs late in the folding process and ...
