Day: February 20, 2015

Upper Peninsula ACS Local Section Research Seminar

Upper Peninsula ACS Local Section Research Seminar

“Carbon Nanomaterials: from Zero-dimensional Cages to Three-dimensional Graphene Sheets “

Dr. Yun Hang Hu,  Charles and Carroll McArthur Endowed Chair Professor
Department of Materials Science and Engineering, Michigan Technological University

February 27, 2015 – 3:00 PM – Rekhi Hall G006

Abstract

Because of the bonding flexibility of carbon, carbon-based materials exhibit various structures with a large variety of physical and chemical properties. Three-dimensional carbon allotropes (graphite and diamond) have been known from the earliest history. The zero-dimensional carbon fullerenes and one-dimensional carbon nanotubes were discovered within the last 30 years. Furthermore, isolated two-dimensional graphene, which is a one-atom thick carbon layer with hexagonal ‘‘honeycomb” lattice, was experimentally obtained 10 years ago. Actually, the discovery of those nano-structured carbon materials is one of the most important developments in science and engineering. In this talk, Dr. Hu is going to discuss his research for (a) the defect structures and the endohedral complexes of C60, (b) the stability and structure of atomic carbon chains, and (c) the synthesis and application of three dimensional graphene sheets and their application for energy.

Biography
Dr. Yun Hang Hu is the inaugural Charles and Carroll McArthur Endowed Chair Professor at
Michigan Technological University. His main research interests range from nanomaterials, CO2 conversion, clean fuels, hydrogen storage materials, catalysis, quantum chemistry calculations to solar energy. He has published more than 120 peer reviewed papers in reputed journals (such as JACS, Angew. Chem. Int. Ed., and Adv. Mater.) and organized more than 20 international symposia on materials and energy. He was a program chair for the ACS Energy and Fuels Division. He is an editor for three books, an editorial board member for nine journals, a chair of the ACS Energy and Fuels Division, and a president of the Hydrogen Storage Division of the International Association of Hydrogen Energy (IAHE). He is a fellow of American Association for the Advancement of Science (AAAS) and the Royal Society of Chemistry (RSC).


Assessing the Binding Capabilities of Bromodomain-Containing Protein 9

Sarah Hopson (Advisor- Dr. Martin Thompson)

Doctoral Student, Department of Chemistry,Michigan Technological University

Monday, March 2, 2015-9:00 am- Admin 404

Abstract

Post-translational modifications of histones, such as the acetylation of lysines, play an importantrole in regulating transcription. Histone tails have a large proportion of positively-charged residues, which create electrostatic interactions with the negatively-charged DNA backbone. Lysine acetylation is thought to weaken these interactions, because it neutralizes lysine’s positively-charged side chain.

Proteins recognize the acetylated lysines using bromodomains; bromodomains are acetylated lysine “readers” and play a critical role in modulation of gene expression. Of the 46 bromodomain-containing proteins in the human proteome, 15 function as transcriptional regulators and 8 function as chromatin remodelers. Nearly all of the other bromodomain proteins influence transcription in some manner (histone acetyltransferase, transcription repressor, transcription initiation, etc.). Due to their significant influence on transcription, mutations of bromodomains are often linked with cancers.

Bromodomain-containing protein 9 (BRD9) has not yet been studied. The aim of this proposed research is to determine the specificity and affinity of BRD9 toward acetyl-lysine sites on the tails of the four core histone proteins.

A high-throughput examination of possible histone interactions with the bromodomain of BRD9 will be conducted using a modified SPOT array. The peptides demonstrating the strongest interactions with the bromodomain will be synthesized using standard Fmoc peptide synthesis. A quantitative examination of the binding affinities of these peptides to the bromodomain, the bromodomain and DUF3512 (domain of unknown function), and the full length BRD9 will be conducted using isothermal titration calorimetry. The results will be compared to determine how the surrounding amino acid sequences affect the bromodomain’s binding capabilities.