Independence and graph homomorphisms graph homomorphisms

A graph with n vertices that contains no triangle and no 5-cycle and minimum degree exceeding n/4 contains an independent set with at least (3n)/7 vertices. This is best possible. The proof proceeds by producing a homomorphism to the 7-cycle and invoking the No Homomorphism Lemma. For k ≥ 4, a graph with n vertices, odd girth 2k+1, and minimum degree exceeding n/(k+1) contains an independent set with at least kn/(2k+1) vertices; however, we suspect this is not best possible. © 1993 John Wiley & Sons, Inc.     

Atomic coherence effects in the ion-trap laser

The influence of atomic coherence effects on the statistical and spectral properties of the ion-trap laser is investigated. Various pump configurations are considered for a realistic level scheme using a Ca ion. Compared to previous suggestions, 50% more output is obtained.     

Design,synthesis, and evaluation of 6-carboxyalkyl and 6-phosphonoxyalkyl derivatives of 7-oxo-8-ribitylaminolumazines as inhibitors of riboflavin synthase and lumazine synthase

A series of 6-carboxyalkyl and 6-phosphonoxyalkyl derivatives of 7-oxo-8-D-ribityllumazine were synthesized as inhibitors of both Escherichia coli riboflavin synthase and Bacillus subtilis lumazine synthase. The compounds were designed to bind to both the ribitylpurine binding site and the phosphate binding site of lumazine synthase. In the carboxyalkyl series, maximum activity against both enzymes was observed with the 3'-carboxypropyl compound 22. Lengthening or shortening the chain linking the carboxyl group to the lumazine by one carbon resulted in decreased activity. In the phosphonoxyalkyl series, the 3'-phosphonoxypropyl compound 33 was more potent than the 4'-phosphonoxybutyl derivative 39 against lumazine synthase, but it was less potent against riboflavin synthase. Molecular modeling suggested that the terminal carboxyl group of 6-(3'-carboxypropyl)-7-oxo-8-D-ribityllumazine (22) may bind to the side chains of Arg127 and Lys135 of the enzyme. A hypothetical molecular model was also constructed for the binding of 6-(2'-carboxyethyl)-7-oxolumazine (15) in the active site of E. coli riboflavin synthase, which demonstrated that the active site could readily accommodate two molecules of the inhibitor.