Heat stress proteins can be assigned to eleven protein families conserved among bacteria, plants and animals. Most of them aid other proteins to maintain or regain their native conformation by stabilizing partially unfolded states. Hence, they are called molecular chaperones. Experimental data indicate that many of them form heterooligomeric complexes, so-called chaperone machines, interacting with each other to generate a network for maturation, assembly and intracellular targeting of proteins. In this review we summarize the essential information on the structure and function of chaperone and chaperone complexes. In addition we present a compilation of in vivo and in vivo test systems used in the preceding ten years of chaperone research.