Small heat shock proteins (sHSPs) belong to a family of 12- to 43-kDaproteins that are ubiquitous and are largely conserved in amino acid sequence among allorganisms. The principal heat-shock proteins that have chaperone activity (that is, they protectnewly made proteins from misfolding) belong to five conserved classes HSP100,HSP90, HSP70, HSP60 and the small heat-shock proteins (sHSPs). The sHSPs (which include alpha crystallin) can form large multimeric structures and have a wide range of cellular functions,including endowing cells with thermotolerance in vivo and being able to act as molecular chaperones in vitro sHSPs do this by forming stable complexes with folding -or unfolding- intermediates of their proteinsubstrates, probably the molten globule. This paper includes a brief survey of the chaperone family, the small heat shock protein superfamily,transcription of sHSPs, sequence comparisons and structural models of small heat shock proteins - structuralelements as potential drug targets, sHSPs as chaperone-like proteins, alpha crystallin chaperone-like activity,conformational diseases - the role of alpha crystallin small heat shock protein superfamily proteins, post-translationalmodification and useful pharmacological agents. Functionality of small heat shock proteins - targets and diseases where pharmacologically active agents are ofimportance, alpha crystallin- small heat shock proteins and prion diseases specific targets for diagnostic testsand drug development, details of some specific small heat shock proteins as drug targets, structural andfunctional implications for treatment.