ausblenden:
Schlagwörter:
RIBULOSE BISPHOSPHATE CARBOXYLASE; MOLECULAR CHAPERONES;
ESCHERICHIA-COLI; POLYPEPTIDE FLUX; ATP HYDROLYSIS; REACTION CYCLE;
TRIGGER FACTOR; CENTRAL CAVITY; PROTEIN; GROELCell Biology;
Zusammenfassung:
Protein folding in the cell was originally assumed to be a spontaneous process, based on Anfinsen's discovery that purified proteins can fold on their own after removal from denaturant. Consequently cell biologists showed little interest in the protein folding process. This changed only in the mid and late 1980s, when the chaperone story began to unfold. As a result, we now know that in vivo, protein folding requires assistance by a complex machinery of molecular chaperones. To ensure efficient folding, members of different chaperone classes receive the nascent protein chain emerging from the ribosome and guide it along an ordered pathway toward the native state. I was fortunate to contribute to these developments early on. In this short essay, I will describe some of the critical steps leading to the current concept of protein folding as a highly organized cellular process.
