We're excited to host the Malina Brothers! An extraordinary fusion of Bluegrass and Baroque music from the Czech Republic.

In 2010 the three Malina brothers, namely banjo player Luboš (oftheaward-winning „Czechgrass“ group Druhá tráva), guitarist Pavel, and violinist Josef, formed their family band Malina Brothers, which was eventually joined by Pavel Peroutka on double bass. All four “Brothers” are natives of Náchod, a city on the Czech-Polish border. They have toured extensively in the USA, as well as on domestic and European stages, and they have collaborated with Czech and international musicians such as Peter Rowan, Charlie McCoy, Béla Fleck and others. The Malina Brothers honour their musical connections to the Eastern-Bohemian Bluegrass and “Tramping” traditions, which were their main influences during the stark years of the Communist regime. The three Malina brothers eventually developed their own, unique musical style based on their listening to American Country and Bluegrass recordings (which would occasionally make their way into Czechoslovakia through the Iron Curtain), combined with the musical influences of the local “Tramping” movement, Eastern European Folklore, and Classical music.

On their latest album, “Baroquegrass 1721-2021” the Malina Brothers introduced a fusion of Bluegrass and Baroque music with a series of original arrangements, creating a brand new musical style: Baroquegrass https://www.youtube.com/watch?v=3mzW_9QWAtE

This event is part of the Many Mountains Fall Festival, check out our full calendar for other events!

Join us for a Work-In-Progress screening and discussion of The Mountain Fiesta: Bridging the Gap & Building Community in Rural Appalachia, featuring filmmakers Roderico Yool-Díaz and Emily (Gibson) Rhyne of Iximché Media at the Niles Gallery on Monday, September 26^th at 5:00pm.  

This event is part of the Many Mountains Fall Festival, check out our full calendar for other events!

The University of Kentucky Army ROTC Wildcat Battalion invites you to the Annual Alumni Breakfast on 17 SEP 22 at the Buell Armory hosted by LTC Alan R. Overmyer and LTC (R) Phil Tilly.  Followed by the Honoring Heroes UK Football game versus Youngstown State.  

Dr. Jeremy Lohman

Abstract: The biosynthesis of both fatty acids and polyketides involves a common reaction, the iterative carbon-carbon bond formation between acyl-thioesters and malonyl-thioesters. While fatty acids and polyketides are essential to society for a plethorea of reasons, how the underlying carbon-carbon bond forming reactions occur remains an open question. Malonyl-thioesters are akin to biochemical hot-potatoes, because they are prone to hydrolysis and decarboxylation. While these two high-energy reactions are exploited by nature for biosynthetic purpose, they plague the structural biologist. We developed molecules that look like malonyl-thioesters but are much more stable, thus we have chilled the hot-potato. These stable malonyl-thioester analogs have provided us with insight into the catalysis of three enzymes. Our preliminary studies with these malonyl-thioester analogs demonstrate that we will be able to generate insight into fatty acid and polyketide biosynthesis, paving the way for new routes to drugs, agrochemicals and biofuels.

Dr. Francis Yoshimoto 

The Yoshimoto research laboratory at UTSA harnesses the power of synthetic chemistry to solve challenging problems relevant to human health.

Artemisinin, one of the topics of the 2015 Nobel Prizes in Medicine, is an endoperoxide-containing sesquiterpenoid plant natural product used to treat malaria. The biosynthesis of the endoperoxide functional group, which gives the natural product its antimalarial activities, has been controversial. Using isotope-labeling strategies, we have elucidated the mechanism of the nonenzymatic endoperoxide forming cascade reaction that converts the precursor, dihydroartemisinic acid, to artemisinin in four steps: (i) first oxygen incorporation, (ii) C-C bond cleavage, (iii) second oxygen incorporation, (iv) and polycyclization to form artemisinin (1,2). Analogs of DHAA have been synthesized to probe endoperoxide formation, which led to the elucidation of the mechanism of the formation of the aromatic ring in serrulatene, an antibiotic plant natural product (3).

Secondly, human cytochrome P450 8B1, the oxysterol-12a-hydroxylase enzyme implicated in bile acid biosynthesis, is a therapeutic target to treat obesity. Preliminary studies involving the synthesis of a rationally designed inhibitor of P450 8B1 through the incorporation of a C12-pyridine in the steroid backbone, will be discussed (4).

1.         Varela, K., Arman, H. D., and Yoshimoto, F. K. (2020) Synthesis of [3,3-²H₂]-Dihydroartemisinic Acid to Measure the Rate of Nonenzymatic Conversion of Dihydroartemisinic Acid to Artemisinin. J. Nat. Prod. 83, 66-78

2.         Varela, K., Arman, H. D., and Yoshimoto, F. K. (2021) Synthesis of [15,15,15-²H₃]-Dihydroartemisinic Acid and Isotope Studies Support a Mixed Mechanism in the Endoperoxide Formation to Artemisinin J. Nat. Prod. 84, 1967-1984

3.         Varela, K., Al Mahmud, H., Arman, H. D., Martinez, L. R., Wakeman, C. A., and Yoshimoto, F. K. (2022) Autoxidation of a C2-Olefinated Dihydroartemisinic Acid Analogue to Form an Aromatic Ring: Application to Serrulatene Biosynthesis. J. Nat. Prod. 85, 951-962

4.         Chung, E., Offei, S. D., Jia, U. A., Estevez, J., Perez, Y., Arman, H. D., and Yoshimoto, F. K. (2022) A synthesis of a rationally designed inhibitor of cytochrome P450 8B1, a therapeutic target to treat obesity. Steroids 178, 108952

Dr. Michele Di Pierro  Di Pierro Lab

Abstract:

The human genome is composed of 46 DNA molecules — the chromosomes — with a combined length of about two meters. Chromosomes are stored in the cell nucleus in a very organized fashion that is specific to the cell type and phase of life; this three-dimensional architecture is a key element of transcriptional regulation and its disruption often leads to disease.  What is the physical mechanism leading to genome architecture? If the DNA contained in every human cell is identical, where is the blueprint of such architecture stored? 

In this talk, I will demonstrate how the architecture of interphase chromosomes is encoded in the one-dimensional sequence of epigenetic markings much as three-dimensional protein structures are determined by their one-dimensional sequence of amino acids. In contrast to the situation for proteins, however, the sequence code provided by the epigenetic marks that decorate the chromatin fiber is not fixed but is dynamically rewritten during cell differentiation, modulating both the three-dimensional structure and gene expression in different cell types.

This idea led to the development of a physical theory for the folding of genomes, which enables predicting the spatial conformation of chromosomes with unprecedented accuracy and specificity. Finally, I will demonstrate how the different energy terms present in our model impact the topology of chromosomes across evolution. Our results open the way for studying functional aspects of genome architecture along the three of life.

Bio:

Michele Di Pierro is Assistant Professor of Physics at Northeastern University and senior investigator of the Center for Theoretical Biological Physics — an NSF Frontier of Physics Center. He studied Condensed Matter Physics at the University of Rome “La Sapienza” and received a PhD in Applied Mathematics from The University of Texas at Austin. Prior to joining Northeastern University, he was the Robert A. Welch Postdoctoral Fellow at Rice University.

His research focuses on the physical processes involved in the translation of genetic information, a branch of biophysics which he refers to as Physical Genetics. His group develops novel theoretical approaches to characterize the structure and function of the genome using the tools of statistical physics, information theory, and computational modeling.