A photochromic azobenzene linker was incorporated as a turn element into an amino acid sequence known to fold into a beta-hairpin structure in aqueous solution. Oligomer formation when the linker was in its thermodynamically favored trans form prohibited structure determination. Light-induced conformational change of the linker to the cis form led to the formation of monomers which exhibited a well-defined P-hairpin structure as determined by H-1 NMR. The rate of the light-induced cis-to-trans isomerization of the azobenzene-containing peptide was 30% slower compared to the unsubstituted chromophore. These results suggest that suitably substituted azobenzenes can be used as photoinclucible turn elements to investigate and control the folding and stability of beta -sheets.