R.P. Beckmann, L.A. Mizzen, W.J. Welch, "Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly," Science, 248:850-54, 1990.
Richard P. Beckmann (Eli Lilly and Co., Indianapolis; formerly at University of California, San Francisco): "Stress proteins were originally identified as a group of proteins whose synthesis is selectively increased or induced after stress. Later it was shown that most stress proteins are synthesized under normal growth conditions and appear essential for survival of both the normal (unstressed) and stressed cell. The excitement regarding stress proteins results from studies indicating that at least some of these proteins are important in facilitating the folding of other cellular proteins.
"Several years ago, C.B. Anfinsen (Science, 181:223-30, 1973) demonstrated that protein folding in vitro is a self-directed process dictated by the primary sequence of amino acids. Currently, it appears that folding in vivo is facilitated by at least two different ...
