Do all wood bats perform the same?

Engineering of Sport 15 - Proceedings from the 15th International Conference on the Engineering of Sport (ISEA 2024) The wood bat is a necessary tool used by batters in professional baseball. The question arises as to whether nominally identical wood bats perform the same, where “nominally identical” means the bats have the same length, weight, weight distribution, and shape. In this context, performance is defined as batted-ball speed under some standard game conditions. Given the constraints, such bats will likely be swung identically, so that the only feature that distinguishes their performance is the bat-ball coefficient of restitution (BBCOR), a measure of energy dissipation in the bat-ball collision. A larger/smaller BBCOR means less/more energy dissipation and consequently a greater/lesser batted-ball speed. While the energy dissipated in the bat-ball collision is primarily in the baseball, the bat also matters in that the collision can transfer energy to the bat in the form of bending vibrations. The latter is especially the case for impacts removed from the so-called sweet spot, which minimizes vibrations and maximizes performance. The objective of the present study is to determine whether there are differences in performance of nominally identical bats and to see how such difference might correlate with differences in the vibrational properties of the bats. The study focuses not only on differences at the sweet spot, but also on differences at other impact locations. </p

Additional file 1: of Complete genomic sequences of Propionibacterium freudenreichii phages from Swiss cheese reveal greater diversity than Cutibacterium (formerly Propionibacterium) acnes phages

Table S1. P. freudenreichii strains used in this study. Table S2. Average nucleotide identities of P. freudenreichii phages. (DOCX 71 kb

Additional file 2: of Complete genomic sequences of Propionibacterium freudenreichii phages from Swiss cheese reveal greater diversity than Cutibacterium (formerly Propionibacterium) acnes phages

Figure S1. Genome organization of phage B22. Predicted genes are shown as boxes either above or below the genome corresponding to rightwards- and leftwards-transcription, respectively. The gene numbers are shown within each colored box and its phamily number is shown above with the number of phamily members shown in parentheses; coloring reflects the phamily assignment. Grouping of genes into phamily of related sequences and map generation was performed using Phamerator (30) and the database ‘Actinobacteriophage_685’. Putative gene functions are listed above the genes. (PDF 164 kb

Additional file 4: of Complete genomic sequences of Propionibacterium freudenreichii phages from Swiss cheese reveal greater diversity than Cutibacterium (formerly Propionibacterium) acnes phages

Figure S3. Genome organization of phage G4. See Additional file 2: Figure S1 for details. (PDF 185 kb

Additional file 7: of Complete genomic sequences of Propionibacterium freudenreichii phages from Swiss cheese reveal greater diversity than Cutibacterium (formerly Propionibacterium) acnes phages

Figure S6. Phylogenetic tree of tandemly repeated genes in P. freudenreichii phages. The four Cluster BW phages all encode two copies of related genes that are tandemly repeated in Doucette, B22, and E6, but which are separated by 17 genes in G4. The Cluster BV phage Anatole contains a single copy of this gene. Genes duplicated in one genome (e.g. Doucette 38 and 39) are more distantly related (51% aa identity) that with the corresponding gene in another genome (e.g. Doucette gp39 and B22 gp38 share 93% aa identity). Sequences were aligned using ClustalX and the tree drawn using NJPlot. Bootstrap values from 1000 iterations are shown. (PDF 22 kb

Additional file 5: of Complete genomic sequences of Propionibacterium freudenreichii phages from Swiss cheese reveal greater diversity than Cutibacterium (formerly Propionibacterium) acnes phages

Figure S4. Genome organization of phage E1. See Additional file 2: Figure S1 for details. (PDF 152 kb

Additional file 6: of Complete genomic sequences of Propionibacterium freudenreichii phages from Swiss cheese reveal greater diversity than Cutibacterium (formerly Propionibacterium) acnes phages

Figure S5. Genome organization of phage B3. See Additional file 2: Figure S1 for details. (PDF 159 kb

Additional file 3: of Complete genomic sequences of Propionibacterium freudenreichii phages from Swiss cheese reveal greater diversity than Cutibacterium (formerly Propionibacterium) acnes phages

Figure S2. Genome organization of phage E6. See Additional file 2: Figure S1 for details. (PDF 161 kb

Design, Synthesis, and Biological Activity of Substrate Competitive SMYD2 Inhibitors

Protein lysine methyltransferases (KMTs) have emerged as important regulators of epigenetic signaling. These enzymes catalyze the transfer of donor methyl groups from the cofactor <i>S</i>-adenosylmethionine to specific acceptor lysine residues on histones, leading to changes in chromatin structure and transcriptional regulation. These enzymes also methylate an array of nonhistone proteins, suggesting additional mechanisms by which they influence cellular physiology. SMYD2 is reported to be an oncogenic methyltransferase that represses the functional activity of the tumor suppressor proteins p53 and RB. HTS screening led to identification of five distinct substrate-competitive chemical series. Determination of liganded crystal structures of SMYD2 contributed significantly to “<i>hit-to-lead</i>” design efforts, culminating in the creation of potent and selective inhibitors that were used to understand the functional consequences of SMYD2 inhibition. Taken together, these results have broad implications for inhibitor design against KMTs and clearly demonstrate the potential for developing novel therapies against these enzymes

Design, Synthesis, and Biological Activity of Substrate Competitive SMYD2 Inhibitors

Protein lysine methyltransferases (KMTs) have emerged as important regulators of epigenetic signaling. These enzymes catalyze the transfer of donor methyl groups from the cofactor <i>S</i>-adenosylmethionine to specific acceptor lysine residues on histones, leading to changes in chromatin structure and transcriptional regulation. These enzymes also methylate an array of nonhistone proteins, suggesting additional mechanisms by which they influence cellular physiology. SMYD2 is reported to be an oncogenic methyltransferase that represses the functional activity of the tumor suppressor proteins p53 and RB. HTS screening led to identification of five distinct substrate-competitive chemical series. Determination of liganded crystal structures of SMYD2 contributed significantly to “<i>hit-to-lead</i>” design efforts, culminating in the creation of potent and selective inhibitors that were used to understand the functional consequences of SMYD2 inhibition. Taken together, these results have broad implications for inhibitor design against KMTs and clearly demonstrate the potential for developing novel therapies against these enzymes