ABSTRACT
Lipocalinology, as a discipline, has been with us for more or less twenty years. After an initial period of exciting, if capricious, growth, study o f the lipocalin protein family has now entered a period o f solid and significant maturity. The modern era o f lipocalin research is marked by the astonishing and burgeoning diversity o f function currendy be coming apparent among members o f this remarkable family. The lipocalins are, perhaps, best known to those outside the field for two notable properties. First, the simplicity and aesthetic appeal o f their highly symmetrical β -barrel fold. Secondly, and more significantly, is the seeming paradox o f their low sequence conservation, which stands in marked contrast to their high structural propinquity.1
