Shaping Authentic Practices by Engaging in Modeling of A Topic with Teachers to Explore Research in Science (SHAPE MATTERS) is funded by the NIH Science Education Partnership Award. The program has three objectives.
Description: Shaping Authentics Practices by Engaging in Modeling of A Topic with Teachers to Explore Research in Science (SHAPE MATTERS) is funded by the NIH Science Education Partnership Award. The program has three objectives.
Director Center for Science and the Schools, Associate Professor of Science Education
As the Director of the Center for Science and the Schools, Dr. Hill serves as the education lead on many technical grants across the STEM colleges at Penn State. In her role, she oversees the development, organization, management, and evaluation of education programs that serve to bridge cutting edge research to K-12 education. Her research focuses on three areas: a) designing professional development programs that engage teachers in the practices of scientists and engineers and promote effective strategies for engaging K-12 students in classroom research projects; b) examining teachers’ pedagogical content knowledge for supporting student-led research projects in the classroom; and c) building outreach programs that bridge the research of STEM faculty and graduate students with K-12 education. Prior to coming to Penn State, Kathy worked as an environmental scientist, science teacher, and Assistant Professor of Education at Bethany College in West Virginia.
STEM Education Outreach Specialist, Doctoral Student Curriculum and Instruction (Science Education)
Amber is a STEM Education Outreach Specialist at the Center for Science and the Schools, former high school biology teacher, and current doctoral student in Science Education at Penn State. In her current role at CSATS, she works with STEM research faculty to design and implement content-specific professional development for teachers that focuses on the practices of scientists and engineers at Penn State. As a doctoral student, her research focuses on a) the intersections of scientific modeling and computing in high school biology classrooms; and b) designing professional development programs that engage teachers in the practices of scientists and engineers. Before coming to Penn State, she taught Biology, Honors Biology, Physical Science, Anatomy and Physiology, and Marine Science for five years. While teaching, she also got involved in leading professional development for science teachers through collaborating with the Milwaukee School of Engineering Center for Biomolecular Modeling in her district and at local and national conferences.
STEM Education Outreach Specialist
Tiffany is a former high school science teacher at Middletown Area High School outside of Harrisburg, PA. In her seven years of teaching, she taught Earth Systems Science, Biology, Advanced Biology, AP Biology, and Forensics. She led building-level professional development sessions and presented at various educational conferences on incorporating research projects in the classroom. Tiffany’s main interest lies in introducing students to authentic science by helping teachers understand how to engage students in the practices of scientists and engineers. Her role at CSATS is to work with research faculty at Penn State to bring current research to the classroom by developing content-specific professional development for teachers. She also engages in building relationships with school districts in the greater Harrisburg area to better support science education.
Associate Professor of Biochemistry and Molecular Biology in the College of Medicine.
Dr. Ropson’s research has focused on the structure, folding, and function of proteins. He has examined the folding mechanism of ß-sheet proteins in the intracellular fatty acid binding protein family using kinetic studies of the fluorescence and circular dichroism spectra as the proteins move from the unfolded to the native state. These proteins have low levels of sequence homology, and there appears to be considerable differences in the path of folding for these sequences to the same final structure. Dr. Ropson has also worked on the effects of mutations on retroviral capsid assembly, and the adaptation of protein function to environmental stresses. He has been involved with teacher molecular structure and modeling to undergraduate, graduate, medical, and high school students.
Associate Professor of Chemistry and of Biochemistry and Molecular Biology at Penn State University Park.
Dr. Boal’s research focuses on understanding the structural differences between members of large metalloenzyme superfamilies that share common features buth promote different reactions or use distinct cofactors. Targets are unified in their ability to activity strong C-H, N-H, or O-H bonds. She characterizes stable reactant and product complexes with an increasing focus on development and implementation of crystallographic approaches to study metalloenzyme reaction intermediates.
Research Professor of Biochemistry and Molecular Biology, Director of X-Ray Crystallography Facility
Dr. Yennawar has collaborated with the research faculty from various departments at the Penn State University Park campus as well as Penn State’s sister campuses. Primarily, Dr. Yennawar has been involved in crystallization, single crystal X-ray data collection at home and synchrotron laboratories, determination and analyzing of three dimensional structures of molecules of interest using X-ray diffraction techniques (small and macromolecular). He has taught the Biomolecular Structure (BMMB 531) course for over a decade.
Associate Professor of Biochemistry and Molecular Biology, Director of the X-Ray Crystallography and Automated Biological Calorimetry Facilities at the Huck Institutes of the Life Sciences
Dr. Yennawar’s research focuses on three key areas at the cusp of materials and life sciences: (1) Atomic resolution structure determination by X-ray crystallography and micro-electron diffraction on a transmission cryo-electron microsome; (2) Designing protein, peptide, and DNA crystals for enhanced nonlinear optical properties for devices; and (3) Biophysical characterization by circular dichroism and transmission electron microscopy of the interfaced formed between DNA and synthetic materials for next generation solar cells and biosensors. She has held frequent training sessions and workshops on all of the biophysical equipment in the lab.
The SHAPE MATTERS program will offer a 10-day professional development workshop for teachers during the summer that will include in-person and virtual meetings. The professional development is geared towards secondary life science and chemistry teachers in Pennsylvania. During the professional development, teachers will collaborate with science education faculty from the Center for Science and the Schools and research scientists from the College of Medicine and the Eberly College of Science. To explore molecular stories related to human health, teachers will engage in research techniques such as crystallization, structure determination, and modeling using the molecular visualization software, Jmol. Teachers will work with the SHAPE MATTERS team to co-construct a molecular modeling research project for their classroom. The research project will support student participation in the SMART teams program.
Secondary life science and chemistry teachers
The application requires general contact information, direct supervisor information, an up-to-date resume, 4 short essay questions, 3 professional references, and a support letter from your immediate supervisor.
Research in the Bevilacqua Lab is centered on understanding functions of RNA in nature at the molecular level. RNA is a fascinating molecule because it has both genetic and functional capabilities. This has led to the notion that RNA was particularly important in the emergence of life on Earth–the “RNA World Hypothesis”. RNA is also of interest because it is involved in a wide range of important biological pathways, recognized most recently as the genetic material of the SARS-CoV-2 virus and the basis of the Moderna and Pfizer mRNA vaccines. We work on RNAs ranging from simple model systems to the entire transcriptome (tens of thousands of RNAs) in living organisms. The project our teachers will be working on will involve recognition of ligands by riboswitches. Riboswitches are a recently discovered class of RNA molecules that specifically and tightly bind small molecules to regulate gene expression. Our teachers will study two closely related purine riboswitches and understand the molecular basis for their specificity. Teachers will learn chemical concepts interfacing with physics and biology, including folding of RNA, molecular recognition of ligands, and regulation of gene expression.
Nearly half of the antibiotics that are currently prescribed target the bacterial ribosome. However, bacteria are rapidly evolving new ways to resist these antibiotics. One emerging mode of enzymatic antibiotic resistance is the structural modification of the ribosome by the radical SAM enzyme Cfr. Radical SAM (RS) enzymes share a common functional motif, an iron-sulfur cluster that coordinates S-adenosylmethionine (SAM), to generate a 5’-deoxyadenosine radical (5’-dA•). The 5’-dA• moiety in RS proteins initiates reactions with substrates by abstracting an H-atom. After Cfr performs this chemically challenging first step, several other steps occur, culminating in the methylation (i.e., the formation of a carbon-carbon bond) of ribosomal ribonucleic acid (RNA). Cfr uses this powerful chemistry to methylate a single site in the bacterial ribosome, the eighth carbon of the adenine ring on A2503. This structural modification inhibits antibiotic binding to the bacterial ribosome conferring antibiotic resistance. In collaboration with Squire Booker’s laboratory, our research focuses on structural determination of Cfr and a related radical SAM methylase, RlmN, to understand how Cfr and RlmN recognize substrate and perform the chemistry associated with RNA modification. To date, we have solved structures of an RNA-bound RlmN intermediate, the first view of a radical SAM enzyme in complex with a large macromolecular substrate.
The ongoing COVID-19 pandemic that is threatening people's lives across the world is underscoring the urgent need to develop effective antiviral agents for SARS-CoV-2, the causative agent of COVID-19. The SARS-CoV-2 main protease Mpro (its alternate name 3C-like protease 3CLpro), which cleaves the viral non-structural polyprotein (NSP) for assembling a replication-transcription complex (RTC), is one of excellent antiviral targets to prevent SARS-CoV-2 replication. The Murakami’s group has been determining the atomic-resolution X-ray crystallographic structure of Mpro in complex with protease inhibitor (Figure below) for understanding the mechanisms of Mpro inhibition by small molecules and for developing new SARS-CoV-2 agents.
In protein biochemistry, it is commonly assumed that a protein’s folded state determines its function. However, data emerging over the past decade conclusively show that approximately one-third of all human protein is not folded and yet these segments of “intrinsically disordered protein” often play essential roles in mediating protein-protein interactions. Thus, the premise motivating my laboratory’s research is that folding is not required to impart unique structural features in proteins that drive their biological functions. For example, the transcription factor Pdx1 regulates the production of insulin in pancreatic β-cells. Accomplishing this crucial function requires reversible formation of protein-protein complexes that either activate or repress Pdx1-stimulated transcription. In this project, the SMART team will explore how the intrinsically disordered C-terminal region of Pdx1 interacts with its negative regulator SPOP, which happens in order to avoid cellular stress associated with unnecessary insulin production when blood glucose levels are low. Analysis of co-crystal structures of Pdx1 peptides bound to SPOP will reveal how disordered proteins with diverse amino acid sequences can adopt functionally equivalent structures when bound to a folded partner. Perhaps unsurprisingly, the pdx1 gene is often mutated in diabetic patients; members of this SMART team will formulate a structure-based hypothesis for the mechanism whereby one diabetes-associated Pdx1 mutant may drive a disease phenotype by disrupting Pdx1-SPOP interactions.
The laboratory of Dr. Christopher Yengo studies molecular motor and cytoskeletal proteins and their role in human disease. The lab is currently focused on myosin motors and the actin cytoskeleton. Biochemical, biophysical, and cell biological approaches are utilized to investigate basic molecular mechanisms of motor based transport, contraction, and organization of the actin cytoskeleton. In the long term, the Yengo lab hopes to develop therapeutic strategies for diseases that impact actomyosin based functions. Specific diseases being investigated are inherited forms of heart disease and deafness.