ALPHA-HELIX MIMICRY OF A BETA-TURN

It is shown here that the three-dimensional arrangement of the amino a cids in an RGDF beta-turn (sequence involved in cell adhesion) resembl es that of an alpha-helix with a shuffled RGDF sequence (i.e. RGXFD). A mini-protein was designed and constructed which arranges the RGXFD s equence into a well defined helical conformation. The designed protein is bioactive and folds into the desired structure as assessed by nucl ear magnetic resonance spectroscopy. The recognition process mediated by a beta-turn can thus be mimicked by an alpha-helix. (C) 1998 Academ ic Press.