S.J. Landry, L.M. Gierasch, "The chaperonin GroEL binds a polypeptide in an a-helical conformation," Biochemistry, 30:7359- 7362, 1991.
Sam Landry (formerly with Southwestern Medical Center, Dallas; currently with Tulane University School of Medicine, New Orleans): "Biophysical chemists studying in vitro protein folding and molecular biologists studying diverse cellular processes, including DNA replication and the heat shock response, have converged on a set of proteins called molecular chaperones, which modulate interactions between protein surfaces. Both the hsp60 and hsp70 families of molecular chaperones bind a variety of non- native proteins. This paper represents an initial effort to answer the questions: What characteristics of a non-native protein are recognized and bound by chaperones; and how can chaperones accommodate diverse primary sequences in order to bind many different proteins?
"We began our studies with the E. coli hsp60 called GroEL and examined its interactions with fragments of a protein, rhodanese, whose in vitro ...
