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Molecular chaperones, many of them so-called heat-shock or stress proteins (hsps), have emerged over recent years as an important topic in cell biology. The functions of these proteins under normal cellular conditions as well as under conditions of stress are the focus of intensive research activity of cell biologists, biochemists, and, more recently, biophysicists. From the wealth of studies available to date, it appears that the major importance of molecular chaperones lies in the area of protein folding. The long-held view that newly synthesized proteins in the cell fold in a largely spontaneous process has been called into question. Although the basic principle that the primary sequence of a protein is sufficient to specify its three-dimensional structure remains unchallenged, protein folding in cells, as opposed to the test tube, depends on helper proteins (Table 1). In this review we focus on the function of the major …