The conformational properties of the N-acetyl-N'-methylamides of the dipeptides lysyl-lysine, lysyl-tyrosine, tyrosyl-lysine, and tyrosyl-tyrosine were studied by means of conformational energy calculations, by n.m.r. measurements in deuterated dimethylsulfoxide, and by circular dichroism in water, methanol, dioxane-water, and trifluoroethanol. Since these four dipeptides occur occasionally as bends in proteins, it was of interest to see whether short-range interactions, acting within the terminally blocked dipeptides, are sufficient to stabilize bend conformations significantly over other conformations. It was found that the four dipeptides exist as ensembles of conformations in solution. Therefore, it appears that longer-range interactions, such as those present in proteins, are required if bend conformations of these dipeptide sequences are to exist as stable conformations. Three of the dipeptides behave rather similarly. Both the CD and the n.m.r. experiments and computations indicate that the fourth (Lys-Tyr) differs from the others. It has a preference for compact conformations that appear to be stabilized by strong favorable interactions, primarily hydrogen bonds, between the tyrosyl and the lysyl side chains. The computations suggest that the presence of these interactions, and hence the existence of preferred conformations, is strongly solvent-dependent, and that these interactions are weakened in aqueous solution.
Download Full PDF Version (Non-Commercial Use)