55 research outputs found

    Ramsey-nice families of graphs

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    For a finite family F\mathcal{F} of fixed graphs let Rk(F)R_k(\mathcal{F}) be the smallest integer nn for which every kk-coloring of the edges of the complete graph KnK_n yields a monochromatic copy of some FFF\in\mathcal{F}. We say that F\mathcal{F} is kk-nice if for every graph GG with χ(G)=Rk(F)\chi(G)=R_k(\mathcal{F}) and for every kk-coloring of E(G)E(G) there exists a monochromatic copy of some FFF\in\mathcal{F}. It is easy to see that if F\mathcal{F} contains no forest, then it is not kk-nice for any kk. It seems plausible to conjecture that a (weak) converse holds, namely, for any finite family of graphs F\mathcal{F} that contains at least one forest, and for all kk0(F)k\geq k_0(\mathcal{F}) (or at least for infinitely many values of kk), F\mathcal{F} is kk-nice. We prove several (modest) results in support of this conjecture, showing, in particular, that it holds for each of the three families consisting of two connected graphs with 3 edges each and observing that it holds for any family F\mathcal{F} containing a forest with at most 2 edges. We also study some related problems and disprove a conjecture by Aharoni, Charbit and Howard regarding the size of matchings in regular 3-partite 3-uniform hypergraphs.Comment: 20 pages, 2 figure

    Optical Gain from InAs Nanocrystal Quantum Dots in a Polymer Matrix

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    We report on the first observation of optical gain from InAs nanocrystal quantum dots emitting at 1.55 microns based on a three-beam, time resolved pump-probe technique. The nanocrystals were embedded into a transparent polymer matrix platform suitable for the fabrication of integrated photonic devices.Comment: 8 pages, 3 figures. This second version is excactly the same as the first. It is resubmitted to correct some format errors appeared in the pdf file of the first versio

    How Protein Stability and New Functions Trade Off

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    Numerous studies have noted that the evolution of new enzymatic specificities is accompanied by loss of the protein's thermodynamic stability (ΔΔG), thus suggesting a tradeoff between the acquisition of new enzymatic functions and stability. However, since most mutations are destabilizing (ΔΔG>0), one should ask how destabilizing mutations that confer new or altered enzymatic functions relative to all other mutations are. We applied ΔΔG computations by FoldX to analyze the effects of 548 mutations that arose from the directed evolution of 22 different enzymes. The stability effects, location, and type of function-altering mutations were compared to ΔΔG changes arising from all possible point mutations in the same enzymes. We found that mutations that modulate enzymatic functions are mostly destabilizing (average ΔΔG = +0.9 kcal/mol), and are almost as destabilizing as the “average” mutation in these enzymes (+1.3 kcal/mol). Although their stability effects are not as dramatic as in key catalytic residues, mutations that modify the substrate binding pockets, and thus mediate new enzymatic specificities, place a larger stability burden than surface mutations that underline neutral, non-adaptive evolutionary changes. How are the destabilizing effects of functional mutations balanced to enable adaptation? Our analysis also indicated that many mutations that appear in directed evolution variants with no obvious role in the new function exert stabilizing effects that may compensate for the destabilizing effects of the crucial function-altering mutations. Thus, the evolution of new enzymatic activities, both in nature and in the laboratory, is dependent on the compensatory, stabilizing effect of apparently “silent” mutations in regions of the protein that are irrelevant to its function

    Fruit-Surface Flavonoid Accumulation in Tomato Is Controlled by a SlMYB12-Regulated Transcriptional Network

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    The cuticle covering plants' aerial surfaces is a unique structure that plays a key role in organ development and protection against diverse stress conditions. A detailed analysis of the tomato colorless-peel y mutant was carried out in the framework of studying the outer surface of reproductive organs. The y mutant peel lacks the yellow flavonoid pigment naringenin chalcone, which has been suggested to influence the characteristics and function of the cuticular layer. Large-scale metabolic and transcript profiling revealed broad effects on both primary and secondary metabolism, related mostly to the biosynthesis of phenylpropanoids, particularly flavonoids. These were not restricted to the fruit or to a specific stage of its development and indicated that the y mutant phenotype is due to a mutation in a regulatory gene. Indeed, expression analyses specified three R2R3-MYB–type transcription factors that were significantly down-regulated in the y mutant fruit peel. One of these, SlMYB12, was mapped to the genomic region on tomato chromosome 1 previously shown to harbor the y mutation. Identification of an additional mutant allele that co-segregates with the colorless-peel trait, specific down-regulation of SlMYB12 and rescue of the y phenotype by overexpression of SlMYB12 on the mutant background, confirmed that a lesion in this regulator underlies the y phenotype. Hence, this work provides novel insight to the study of fleshy fruit cuticular structure and paves the way for the elucidation of the regulatory network that controls flavonoid accumulation in tomato fruit cuticle

    The Israeli summer seminars for CS leading teachers

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