Newswise PHILADELPHIA Kristen W. Lynch, PhD, has been appointed chair of the Department of Biochemistry and Biophysics, in the Perelman School of Medicine at the University of Pennsylvania, following eight years as a tenured faculty member in the department.

Dr. Lynch has a broad vision of the future of biochemistry and biophysics at Penn, said J. Larry Jameson, MD, PhD, executive vice president of the University of Pennsylvania for the Health System and dean of the Perelman School of Medicine. Her experience, talent, and collaborative spirit will foster strong ties among investigators within the department, as well as across Penn Medicine and the University. I am confident that under Dr. Lynchs leadership Penn will secure its place among the nations top biochemistry and biophysics departments.

Lynch, who is a professor of Biochemistry and Biophysics, also holds a secondary appointment in the department of Genetics and has expertise in RNA biology and immunology. Her laboratory focuses on understanding the biochemical mechanisms and regulatory networks that control alternative gene splicing in response to antigens. (Antigens are toxins and foreign substances, such as bacteria, viruses, and cells of transplanted organs, that stimulate the production of antibodies to protect an organism.)

Alternative splicing is a process in which a single gene codes for differentbut related forms of a given protein (called isoforms), each of which has similar functions. It eliminates the need for an organism to have large numbers of genes make distinctive proteins for carrying out similar functions throughout the body. Additionally, alternative splicing helps explain why humans have substantial genetic similarity with animals and insects, for example, yet such obvious physical and behavioral differences.

The Lynch laboratory specializes in understanding how alternative splicing is regulated in T cells when the cells are stimulated by an antigen during an immune response. Lynch and her team have identified more than 500 genes that undergo alternative splicing in response to T cell stimulation and have discovered some of the molecular mechanisms and signaling pathways that lead to this regulation.

She received her doctorate from Harvard University in 1996 and completed her postdoctoral training at the University of California, San Francisco. Lynch joined the Penn faculty as an associate professor in the department of Biochemistry and Biophysics in 2009, having been recruited from University of Texas Southwestern Medical Center, where she chaired the biological chemistry graduate program.

She is the author of more than 50 scientific papers in the leading journals in her field and the recipient of numerous awards and honors in recognition of her scientific achievements, including a National Science Foundation Career Award. Lynch founded and directs the campus-wide RNA Group, a central forum for investigators in and around Penn interested in RNA-related topics. Lynch has served as a director of the RNA Society, an international scientific organization; is an editor for Molecular and Cellular Biology; and has co-chaired several international meetings in the field of RNA processing.

Penn Medicine is one of the world's leading academic medical centers, dedicated to the related missions of medical education, biomedical research, and excellence in patient care. Penn Medicine consists of the Raymond and Ruth Perelman School of Medicine at the University of Pennsylvania (founded in 1765 as the nation's first medical school) and the University of Pennsylvania Health System, which together form a $5.3 billion enterprise.

The Perelman School of Medicine has been ranked among the top five medical schools in the United States for the past 18 years, according to U.S. News & World Report's survey of research-oriented medical schools. The School is consistently among the nation's top recipients of funding from the National Institutes of Health, with $373 million awarded in the 2015 fiscal year.

The University of Pennsylvania Health System's patient care facilities include: The Hospital of the University of Pennsylvania and Penn Presbyterian Medical Center -- which are recognized as one of the nation's top "Honor Roll" hospitals by U.S. News & World Report -- Chester County Hospital; Lancaster General Health; Penn Wissahickon Hospice; and Pennsylvania Hospital -- the nation's first hospital, founded in 1751. Additional affiliated inpatient care facilities and services throughout the Philadelphia region include Chestnut Hill Hospital and Good Shepherd Penn Partners, a partnership between Good Shepherd Rehabilitation Network and Penn Medicine.

Penn Medicine is committed to improving lives and health through a variety of community-based programs and activities. In fiscal year 2015, Penn Medicine provided $253.3 million to benefit our community.

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RNA Biologist Kristen Lynch Appointed Chair of Department of Biochemistry and Biophysics at Penn - Newswise (press release)

In biochemistry and pharmacology, a ligand is a substance that forms a complex with a biomolecule to serve a biological purpose. In protein-ligand binding, the ligand is usually a molecule which produces a signal by binding to a site on a target protein. The binding typically results in a change of conformation of the target protein. In DNA-ligand binding studies, the ligand can be a small molecule, ion,[1] or protein[2] which binds to the DNA double helix. The relationship between ligand and binding partner is a function of charge, hydrophobicity, and molecular structure. The instance of binding occurs over an infinitesimal range of time and space, so the rate constant is usually a very small number.

Binding occurs by intermolecular forces, such as ionic bonds, hydrogen bonds and Van der Waals forces. The association of docking is actually reversible through dissociation. Measurably irreversible covalent bonding between a ligand and target molecule is atypical in biological systems. In contrast to the definition of ligand in metalorganic and inorganic chemistry, in biochemistry it is ambiguous whether the ligand generally binds at a metal site, as is the case in hemoglobin. In general, the interpretation of ligand is contextual with regards to what sort of binding has been observed. The etymology stems from ligare, which means 'to bind'.

Ligand binding to a receptor protein alters the chemical conformation by affecting the three-dimensional shape orientation. The conformation of a receptor protein composes the functional state. Ligands include substrates, inhibitors, activators, and neurotransmitters. The rate of binding is called affinity, and this measurement typifies a tendency or strength of the effect. Binding affinity is actualized not only by host-guest interactions, but also by solvent effects that can play a dominant, steric role which drives non-covalent binding in solution.[3] The solvent provides a chemical environment for the ligand and receptor to adapt, and thus accept or reject each other as partners.

Radioligands are radioisotope labeled compounds are used in vivo as tracers in PET studies and for in vitro binding studies.

The interaction of most ligands with their binding sites can be characterized in terms of a binding affinity. In general, high-affinity ligand binding results from greater intermolecular force between the ligand and its receptor while low-affinity ligand binding involves less intermolecular force between the ligand and its receptor. In general, high-affinity binding results in a higher degree of occupancy for the ligand at its receptor binding site than is the case for low-affinity binding; the residence time (lifetime of the receptor-ligand complex) does not correlate. High-affinity binding of ligands to receptors is often physiologically important when some of the binding energy can be used to cause a conformational change in the receptor, resulting in altered behavior of an associated ion channel or enzyme.

A ligand that can bind to a receptor, alter the function of the receptor, and trigger a physiological response is called an agonist for that receptor. Agonist binding to a receptor can be characterized both in terms of how much physiological response can be triggered and in terms of the concentration of the agonist that is required to produce the physiological response. High-affinity ligand binding implies that a relatively low concentration of a ligand is adequate to maximally occupy a ligand-binding site and trigger a physiological response. The lower the Ki concentration is, the more likely there will be a chemical reaction between the pending ion and the receptive antigen. Low-affinity binding (high Ki level) implies that a relatively high concentration of a ligand is required before the binding site is maximally occupied and the maximum physiological response to the ligand is achieved. In the example shown to the right, two different ligands bind to the same receptor binding site. Only one of the agonists shown can maximally stimulate the receptor and, thus, can be defined as a full agonist. An agonist that can only partially activate the physiological response is called a partial agonist. In this example, the concentration at which the full agonist (red curve) can half-maximally activate the receptor is about 5 x 109Molar (nM = nanomolar). Ligands that bind to a receptor but fail to activate the physiological response are receptor antagonists.

In the example shown to the left, ligand-binding curves are shown for two ligands with different binding affinities. Ligand binding is often characterized in terms of the concentration of ligand at which half of the receptor binding sites are occupied, known as the IC50, which is related to but different from the dissociation constant. The ligand illustrated by the red curve has a higher binding affinity and smaller Kd than the ligand illustrated by the green curve. If these two ligands were present at the same time, more of the higher-affinity ligand would be bound to the available receptor binding sites. This is how carbon monoxide can compete with oxygen in binding to hemoglobin, resulting in carbon monoxide poisoning.

Binding affinity is most commonly determined using a radiolabeled ligand, known as a tagged ligand. Homologous competitive binding experiments involve binding competition between a tagged ligand and an untagged ligand.[4] Non-labelled methods such as surface plasmon resonance, dual polarization interferometry and Multi-Parametric Surface Plasmon Resonance (MP-SPR) can not only quantify the affinity from concentration based assays; but also from the kinetics of association and dissociation, and in the later cases, the conformational change induced upon binding. MP-SPR also enables measurements in high saline dissociation buffers thanks to a unique optical setup. Microscale Thermophoresis (MST), an immobilization-free method[5] was developed. This method allows the determination of the binding affinity without any limitation to the ligand's molecular weight.[6]

For the use of statistical mechanics in a quantitative study of the ligand-receptor binding affinity, see the comprehensive article[7] on the configurational partition function.

Binding affinity data alone does not determine the overall potency of a drug. Potency is a result of the complex interplay of both the binding affinity and the ligand efficacy. Ligand efficacy refers to the ability of the ligand to produce a biological response upon binding to the target receptor and the quantitative magnitude of this response. This response may be as an agonist, antagonist, or inverse agonist, depending on the physiological response produced.[8]

Selective ligands have a tendency to bind to very limited kinds of receptor, whereas non-selective ligands bind to several types of receptors. This plays an important role in pharmacology, where drugs that are non-selective tend to have more adverse effects, because they bind to several other receptors in addition to the one generating the desired effect.

Bivalent ligands consist of two drug-like molecules (pharmacophores or ligands) connected by an inert linker. There are various kinds of bivalent ligands and are often classified based on what the pharmacophores target. Homobivalent ligands target two of the same receptor types. Heterobivalent ligands target two different receptor types. Bitopic ligands target an orthosteric binding sites and allosteric binding sites on the same receptor.

In scientific research, bivalent ligands have been used to study receptor dimers and to investigate their properties. This class of ligands was pioneered by Philip S. Portoghese and coworkers while studying the opioid receptor system.[9][10][11] Bivalent ligands were also reported early on by Micheal Conn and coworkers for the gonadotropin-releasing hormone receptor.[12][13] Since these early reports, there have been many bivalent ligands reported for various GPCR systems including cannabinoid,[14] serotonin,[15][16] oxytocin,[17] and melanocortin receptor systems.[18][19][20]

Bivalent ligands usually tend to be larger than their monovalent counterparts, and therefore, not drug-like. (See Lipinskis rule of five.) Many believe this limits their applicability in clinical settings.[21][22] In spite of these beliefs, their have been many ligands that have reported successful per-clinical animal studies.[19][23][24][25][26][27] Given that some bivalent ligands can have many advantages compared to their monovalent counterparts (such as tissue selectivity, increased binding affinity, and increased potency or efficacy), bivalents may offer some clinical advantages as well.

A privileged scaffold[28] is a molecular framework or chemical moiety that is statistically recurrent among known drugs or among a specific array of biologically active compounds. These privileged elements[29] can be used as a basis for designing new active biological compounds or compound libraries.

Main methods to study proteinligand interactions are principal hydrodynamic and calorimetric techniques, and principal spectroscopic and structural methods such as

Other techniques include: fluorescence intensity, bimolecular fluorescence complementation, FRET (fluorescent resonance energy transfer) / FRET quenching surface plasmon resonance, bio-layer interferometry, Coimmunopreciptation indirect ELIS, equilibrium dialysis, gel electrophoresis, far western blot, fluorescence polarization anisotropy, electron paramagnetic resonance, microscale thermophoresis

The dramatically increased computing power of supercomputers and personal computers has made it possible to study proteinligand interactions also by means of computational chemistry. For example, a worldwide grid of well over a million ordinary PCs was harnessed for cancer research in the project grid.org, which ended in April 2007. Grid.org has been succeeded by similar projects such as World Community Grid, Human Proteome Folding Project, Compute Against Cancer and Folding@Home.

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Ligand (biochemistry) - Wikipedia

March 31, 2017 Credit: University of Oxford

An Oxford University spinout company is developing a molecular superglue for the rapid development of vaccines targeting a range of diseases.

SpyBiotech is using 'biochemical superglue' that can facilitate the rapid development of robust and novel vaccines. The company has raised 4m at launch in seed financing to develop the technology, led by Oxford Sciences Innovation with participation from GV.

The company gets its name from the bacterium Streptococcus pyogenes (Spy), the same organism behind a number of infections including strep throat and impetigo. The team behind SpyBiotech divided Spy into a peptide, SpyTag, and a protein partner, SpyCatcher. Naturally attracted to each other, the two form a covalent bond once combined.

SpyBiotech believes that this bond is the missing link to effective development and production of highly effective vaccines. The company will initially focus on virus-like particles (VLPs), a leading technology to induce immune responses by vaccination. Discovered in 1963, VLPs have become a cornerstone of a number of vaccines. Resembling viruses but without pathogenic material, VLPs can instead be coated with bug-busting antigens. However, the two most common ways in which a VLP can be paired with antigens genetic fusion and chemical conjugation are imprecise, expensive, prone to being misassembled, and consequently can result in the failure of a vaccine.

Conversely, SpyBiotech's SpyVLP can be easily and efficiently combined with a number of antigens, and used to produce stable vaccines that induce robust antibody responses. The company plans to target infectious diseases including major viral infections at first, with a view to developing SpyVLP into a universal platform that can be adapted to target a wide variety of conditions. In particular, owing to the versatile and easy-to-use nature of SpyVLP, the technology could underpin efforts to rapidly combat future outbreaks and pandemics.

SpyBiotech will use the seed funding to get its first candidates ready for Phase I trials. During that period, SpyBiotech's founders will receive support from its investors. The founders are aiming to start a further round of funding in the near future to catalyse the development of SpyVLP and expand into other disease areas. A leadership team, including the company's first CEO, will be announced in the coming months.

Sumi Biswas, Associate Professor at the Jenner Institute, Oxford University, said: 'Researchers in the vaccine field, including us, have struggled to make effective VLPs against many diseases for a long time. We view this superglue technology as a game changer to enable faster development of effective vaccines against major global diseases. We are excited to begin the journey of taking this versatile and innovative approach forward and moving our new vaccines from the laboratory to human clinical testing.'

Oxford Sciences Innovation (OSI), the patient capital investor for Oxford University, led the 4m investment, with GV (formerly Google Ventures), an independent venture capital arm of Alphabet, joining in participation.

Lachlan MacKinnon, Principal at OSI, said: 'We see the Spy technology as the missing link in rapid and robust VLP vaccine design and see GV as a natural co-investment partner to take this forward. We are privileged to be working with four founders who bring such an impressive combination of academic prowess and clinical stage experience to the company.'

Tom Hulme, General Partner at GV, added: 'SpyBiotech has established a novel approach using platform VLP vaccine technology that shows promise in a number of addressable markets. We're looking forward to working with a team of world class scientists with extensive experience in vaccine development spanning from vaccine design through to Phase II clinical trials to develop more effective vaccines for a wide range of global diseases.'

The research underpinning SpyBiotech was developed in conjunction between researchers at Oxford University's Department of Biochemistry and Jenner Institute, with four academics joining SpyBiotech at launch. The team includes: Mark Howarth, Professor of Protein Nanotechnology; Sumi Biswas, Associate Professor of Vaccinology; Simon Draper, Professor of Vaccinology; and Dr. Jing Jin. Combined, the founding team has taken twelve products to Phase I and II trials; filed nine patents on vaccines and other technologies; and has extensive experience in biotech and industrial collaborations and partnerships. The commercialisation of SpyBiotech's technology and company formation is supported by Oxford University Innovation, the research commercialisation company of Oxford University.

Carolyn Porter, Deputy Head of Technology Transfer at Oxford University Innovation, said: 'SpyBiotech punctuates research that's been developing for some time here at Oxford, and is a testament to the benefits of collaboration between our departments and institutes. Oxford is playing a leading role in developing the next generation of vaccines, and SpyBiotech and other spinouts working in this sector showcases the potential impact the University can have on the wider world.'

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The Jenner Institute at Oxford University, together with partners Imaxio and GSK, has started a phase I clinical trial of a novel vaccine candidate aimed at blocking transmission of malaria.

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A new method to produce a stable fragment of poliovirus could enable safer production of vaccines, according to a study published in PLOS Pathogens.

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Some genetic mutations can cause a virus to flourish. Others make the virus wither away, unable to function normally and reproduce. Yet other genetic mutations only show their hand under certain conditions.

(Phys.org)A team of chemists at the University of California has developed a cheaper way to functionalize unactivated alkanes (hydrocarbons such as ethane, methane and propane) by using much more abundant catalysts. In ...

High energy, ultraviolet radiation from the Sun is a known to hazard to life, yet the energy provided by our star has played an important role as the essential driver of life on Earth.

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Ceramic textiles, improved jet engine blades, 3-D printed ceramics and better batteries may soon become a reality, thanks to a recently patented polymer from a Kansas State University engineer.

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UNIVERSITY PARK, Pa. Paul Babitzke, professor of biochemistry and molecular biology at Penn State, has been elected as a Fellow of the American Academy of Microbiology. Election as a Fellow recognizes members of the American Society for Microbiology (ASM) who display excellence, originality and leadership and have made exceptional contributions to the advancement of microbiology.

Babitzke's research focuses on the regulation of gene expression where and when genes are used in a cell by RNA structure and RNA-binding proteins. He is interested in the fundamental mechanisms elongation and termination of how RNA molecules are transcribed from DNA, in addition to investigating a variety of genes in which RNA binding proteins control gene expression by transcription attenuation, repression of translation initiation, and/or mRNA stability.

Babitzke has been director of the Biochemistry, Microbiology, and Molecular Biology Graduate Program at Penn State since 2013 and director of the Center for RNA Molecular Biology in the Penn State Huck Institutes of the Life Sciences since 2009. He was elected as a Fellow of the American Association for the Advancement of Science in 2017 and is a member of the ASM, the American Society for Biochemistry and Molecular Biology, and the RNA society. He was the keynote speaker at the Federation of European Biochemical Societies - American Society for Microbiology Conference on the Biology of RNA in host-pathogen interactions in Tenerife, Canary Islands, Spain in 2014 and was honored with the Daniel R. Tershak Memorial Teaching Award in 2009.

Babitzke joined the faculty at Penn State as an assistant professor of biochemistry and molecular biology in 1994, became associate professor in 2000, and professor in 2006. Prior to that, he was a postdoctoral researcher in the Department of Biological Sciences at Stanford University from 1991 to 1994. Babitzke earned a doctoral degree in genetics at the University of Georgia in 1991 and a bachelors degree in biomedical science at St. Cloud State University in Minnesota in 1984.

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Paul Babitzke elected as Fellow of the American Academy of Microbiology - Penn State News

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Two Lubbock Christian University alumni, as well as several undergraduate students and faculty, are presenting at the LCU Scholars Colloquium on Thursday and Friday.

The Scholars Colloquium serves as a forum for undergraduate research and scholarly presentations by LCU students.

Matt Joyner, another LCU alumnus and assistant professor of biochemistry at Pepperdine University, teaches biochemistry and investigates the chemical and pharmacological properties of native medicinal plants used by local American Indians. His presentation will be offered in the Baker Conference Center at 10:45 a.m. on Friday.

The colloquium has become a grand tradition of honoring our students and faculty for their research, and a way to show the larger community that the academic quest at LCU is strong and vibrant, said Stacy Patty, director of LCUs Honors Program and a professor of religion.

Crystal Silva-McCormick, a graduate of LCU and a doctoral candidate in Interfaith Relations at the Lutheran School of Theology in Chicago, will be addressing issues of injustice, particularly among those poor and marginalized in society, and how poverty is interrelated to both injustice and economic disadvantages. Her presentation is scheduled for Thursday at 7 p.m., and it will be given in the Collier Auditorium in the Talkington Center for Nursing Education.

In addition to the keynote addresses, there will be more than 90 presentations and posters during the Scholars Colloquium, a combination of seniors doing capstone projects and other students presenting findings from their scholarly research at the undergraduate level. LCU faculty will also make research presentations.

All presentations are free and open to the public. Please see lcu.edu/scholars for the full Scholars Colloquium schedule.

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2 alumni to present at Lubbock Christian U's Scholars Colloquium - LubbockOnline.com

Date: 03/30/2017 Writer: Taylor Vancel, 575-646-7953, tvancel@nmsu.edu Facebook Twitter LinkedIn Google+ Pinterest

Angelique Amado is a junior at New Mexico State University majoring in chemistry. Thanks to a program that pays undergraduate students to conduct research, she can spend time in the lab without worrying about working off campus to help with school expenses.

Its very hard to balance a job on top of research and activities and academics, said Amado, So having the ability to merge a job and research is awesome because it helps build skills youll need in the future while being able to support yourself financially.

The Discovery Scholars Program in the College of Arts and Sciences has provided paid research opportunities for 25 undergraduate students since it began two years ago.

Through the research experience, Discovery Scholars gain not only highly technical research experience, but also practical experience in working on a project with a team, writing in their field, presenting their results at conferences, and day-to-day project management, said Nancy McMillan, Regents Professor in geology and director of the program.

Feifei Li, assistant professor in chemistry and biochemistry, told Amado about the program. Li has been mentoring Amado in the lab for just over a year.

Amado and Li have taken on two different projects: The first was researching the Vitamin B-12 complex to model how plants intake CO2 and reduce it to carbon monoxide; the second involves data analysis from results of X-ray spectroscopy. The overall goal of this project is to gain a deeper understanding of bioinorganic substances in order to solve bioenergy and biomedical related issues facing society.

As a mentor and teacher, Ive been able to help teach and train chemistry students, Li said. We are training the next generation of leaders in energy science and biomedical fields.

So far, our projects have been pretty successful and Ive been able to learn a lot that I dont always get in class, as well as gaining experience in the lab, Amado said. Ive always been interested in research fields but the program has solidified that in many ways. Im excited to start applying to programs with this experience on my resume.

As a mentor himself, Michael Hout, assistant professor of psychology and assistant director of the program, has seen the impact of the program on students first hand.

I've never seen a program like this implemented anywhere else, and I'd have absolutely loved to be able to take part in something like this when I was an undergraduate. This program affords our students with opportunities that the vast majority of students could not obtain in any other way.

Other Discovery Scholars and mentors in the program currently include astronomy professor Chris Churchill and physics undergraduate, Roberto Araujo are working on uncovering the element berylium from a quasar; Greg Armfield, associate professor of communication studies and communications studies undergraduate, Rachel Simeon, are studying how women are portrayed in sports magazines, professor Elba Serrano and biology undergraduate Taylor Nunn researching how brain cancer cells feel their environment, McMillan and Geology undergraduate Shoshauna Farnsworth-Pinkerton are developing a method to determine the source of ancient sands using the mineral tourmaline and Hout and psychology undergraduate John DesGeorges are studying how humans automatically think of computer- related things when presented with challenging information and questions.

In addition to the research experience, the program also allows students to engage in community service each semester.

This semester weve started working with K-12 students in Las Cruces to show them what its like to do research, Amado said. We want to inspire them to go to college and to maybe pursue some kind of research while there.

Along with going into the public schools, Amado and Li have been working closely with the TRIO program. TRIO is a group of federally funded outreach and student services programs targeted to serve and assist low-income individuals, first-generation college students, and individuals with disabilities to progress through the academic pipeline from middle school to post baccalaureate programs.

Each Discovery Scholar receives $10 per hour for up to 40 hours a week to work on independent, but guided, research with a faculty mentor. For the fall and spring semesters, students receive the same pay for up to 20 hours a week. Funding for the program comes from the College of Arts and Sciences distance education revenue. Students also receive a book fund each semester they participate, including the summer while faculty members receive another fund toward scholarship, creative activity or for conference travel.

Personally, the best aspect of this experience is being given the opportunity to travel to other laboratories and use resources not immediately available in this area, said Amado. I am fortunate enough to be supported by this program to expand my skill set in settings I would not otherwise be able to.

Amado plans to pursue a doctorate in environmental chemistry or bioinorganic chemistry. Shes also considering law school to work with science and policy.

Im really thankful for my time in this program, Amado said. And for the opportunities to help undergraduate students, such as myself, in almost all areas of study.

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UNE Academic Calendars| UNE Academic Catalog|Technical Requirements

This is a one-semester online Biochemistry course designed for individuals who need first semester Biochemistry as a prerequisite to apply for admission to a program in the health professions.

Graduate programs that may require a CHEM 1005 Medical Biochemistry class include:

Medical Biochemistry is a four credit hour course designed to lay the foundation for other basic and clinical medical sciences. The goal of this course is to learn the core concepts of biochemistry that apply to human health and disease and to cite specific examples of their application. You will be able to analyze and evaluate the most common biochemistry cited in medical literature. Furthermore, these basics will facilitate further learning in biochemistry and the health sciences.Click here for the online Biochemistry course syllabus.More detailed readings are available on Blackboard.

The typical student will complete this online Biochemistry course in approximately 16 weeks. Many students are nontraditional students who have elected an online course for flexibility. Since the course is self-paced, you may complete the course in fewerthan 16 weeks.

One semester of college level biology, and one year of chemistry that includes one semester of organic chemistry.All prerequisite courses must have been completed successfully within the past seven years.

To learn more about the technical requirements for this and other Post-Baccalaureate courses, click here.

Credits: 4 Tuition: $1320 Registration: $25 Total: $1345

The cost of the materials is not included in this total.

All exams are taken online. Major exams are required to be proctored. For instructions on how to take your exams online, visit Online Learning's ProctorU site.

You may enroll at any time via our self-service registration portal.Please keep in mind that courses start on the 1st and 3rd Wednesdays of the month. Payment is due in full atthe time of registration. Your official start date is the date that the course opens, and you will have 16 weeks from that date to complete your course.

You must be registered for yourclass by 12:00 noon EST on the Mondaybefore the class starts.See the UNEAcademic Calendarfor more details.

If you have any questions or need help with registering for your class, please callan Enrollment Counselorat1-855-325-0894, email prehealth@une.edu, or view the online FlexReg course registration tutorial.

If you intend to useVA Benefits or Military Tuition Assistance, please do not usethe self-registration portal. Please call 1-855-325-0894 to be directed to the appropriate office for assistance.

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A dozen University of Delaware students (undergraduate and graduate) and alumni have won National Science Foundation Graduate Research Fellowships as the prestigious competition marks its 65th year. Fourteen others received honorable mention designations.

The awards -- for which more than 13,000 applicants competed this year -- include three years of funding at $34,000 per year, plus $12,000 in cost-of-education allowances to the school for study leading to a master's or doctoral degree in science and engineering. The total of these awards is almost $1.4 million -- a significant boost for the students and their research.

"Research is incredibly important," said Dianna Kitt, a senior majoring in environmental engineering and one of UD's 12 winners. "On a large scale, research is what drives our society and allows us to create new technologies and processes that protect humans, animals and the environment. On a smaller scale, research pushes you as an individual to think outside of the book and answer problems that no one else has answered before."

The awards make a powerful statement about these students, said Donald Watson, associate professor of chemistry and biochemistry and the department's associate chair for graduate studies. That department had four winners - two undergraduates and two graduate students - including doctoral student Sarah Krause in Watson's research group.

"This includes all fields of science and engineering and these awards go to extraordinarily high-quality students," he said. "It recognizes their ability and frees students to do science. And getting multiple awards in a single year is a mark of quality for our program."

Nationally, there were 2,000 winners (about 15 percent of all applicants), representing 449 different schools, all 50 states, the District of Columbia and other U.S. territories. Winners included 1,158 women, 498 individuals from underrepresented minority groups and 726 undergraduate seniors.

"This is one of the most prestigious awards a student can get," said Julie Maresca, assistant professor of civil and environmental engineering and Kitt's faculty mentor. "These awards are highly competitive and truly a recognition of the students' potential for future success.

"The students who get these fellowships have demonstrated not only that they are among our top students, but also that they can convincingly propose a multiyear research project and are committed to broadening participation in their fields."

* Ian Berke of Albany, New York, who earned his bachelor's in biomedical engineering in 2016 and now is pursuing a doctoral degree in biomedical engineering at Washington University in St. Louis, Missouri.

"In my sophomore year at UD, I had a sports-related knee injury that required surgery (ACL tear). This got me interested in orthopedic research and I was paired with Christopher Price, assistant professor in biomedical engineering, for a summer scholar research opportunity, in imaging. During the summer and in the following year or so we imaged bone and cartilage using refractive index matching techniques. Dr. Price really sparked my interest in the field and showed me the many avenues researchers were taking to combat osteoarthritis."

* Hannah Clipp of Bel Air, Maryland, who earned two bachelor's degrees -- in wildlife and fisheries resources and multidisciplinary studies -- at West Virginia University and is pursuing a master's degree in wildlife ecology at UD.

The focus of her research is bird migration and stopover ecology and bird conservation.

* Jonathan Galarraga of Belcamp, Maryland, a du Pont Scholar who earned an honors bachelor's degree in chemical engineering in 2016 and will pursue his doctorate at the University of Pennsylvania, where he will study tissue engineering, biomaterials, 3D-printing and cartilage repair.

"Biomaterials are changing possibilities for medicine and healthcare across the world because they provide new avenues for exploring prospective therapeutics, modeling disease pathology and assessing drug toxicity.In my Ph.D. thesis, I will develop new materials approaches for tissue repair through rational material design and impact society through new product development.As a Ph.D. student in Dr. Jason Burdicks Polymeric Biomaterials Lab at the University of Pennsylvania, I am eager to establish strong relationships with leading experts in the country so that I may design and deliver clinically viable biomaterials."

At UD, Galarraga worked in the research group of Christopher Kloxin, assistant professor of chemical and biomolecular engineering.

"Throughout my time in the CJK lab, I gained a strong appreciation for collaborations in research, developed intimate knowledge of the materials science research landscape, and enjoyed the privilegeof learning from many great mentors.

"The aims of my career are to conduct research on biomaterials and bring clinically viable biotechnology to market while teaching as a university professor. In doing so, I will improve the quality of life for people with disabilities and diseases, increase the U.S. competitiveness in the growing biomedical device industry and improve the prospects for future biomedical research. In addition to commercially developing these technologies, I will employ my bioengineering expertise to help develop and implement policies that will ensure that future biomaterials are readily accessible and disseminated to underserved patient populations."

* Nicholas Geneva of Owings, Maryland, an honors degree candidate who is completing his bachelor's degree in mechanical engineering and will pursue a doctoral degree, continuing his work integrating state-of-the-art computer technology and engineering at UD.

"Working with Dr. Lian-Ping Wang [professor of mechanical engineering] and his graduate students is largely the reason why I decided to pursue a Ph.D. His work has shown me that the integration of state-of-the-art computer hardware and engineering is a very important challenge that is facing the scientific community today. Computing, whether through traditional CPUs or other hardware accelerators, is becoming ever more powerful, but exploiting this power effectively to solve the difficult engineering problem is by no means trivial."

* Rebekah Houser of Newark, Delaware, who earned a bachelor's degree in electrical engineering and will continue research on vehicle-to-grid technology and firmware for an infrared scene projector.

"Electric vehicles equipped with vehicle-to-grid technology can provide valuable services to electric power generation and distribution systems. These services promote adoption of electric vehicles and facilitate increased incorporation of renewable resources into the electric power grid. Infrared scene projectors enable more efficient testing of infrared imaging systems that serve as critical tools for first responders, law enforcement and military personnel."

* Dianna Kitt of Aberdeen, Maryland, a du Pont scholar who is completing her bachelor's honors degree with distinction in environmental engineering and will pursue graduate-level research in water treatment.

"I grew up near the Chesapeake Bay so I have always been passionate about clean water and the environment. When I was in high school, I was inspired by my AP biology teacher (who was actually a retired research scientist) to work in a research lab for the first time and I fell in love with research. I knew that I wanted to pursue my passion for improving the environment as my career, and I knew that a career in environmental engineering research would allow me to not only study the environment but also develop techniques and processes to protect it."

* Jodi Kraus of Monument, Colorado, who earned her bachelor's degree at Drexel University and is a second-year grad student in chemistry and biochemistry at UD.

In the laboratory of Tatyana Polenova, professor of chemistry and biochemistry, she has focused on determining the atomic-level structure and dynamics of actin-associated protein assemblies using the technique Magic Angle Spinning NMR.

"I was drawn to using solid-state NMR spectroscopy to study large protein assemblies because the scientific understanding of fundamental biological processes is rapidly expanding, and it is of utmost importance to continue developing new methodologies to study these complex systems. I believe that in order to fully understand these biological processes and identify new potential drug targets (in the case of disease), we must investigate their most basic properties. Additionally, I am interested in methods development and instrumentation because I personally find it gratifying to track the exact physical dynamics which correlate to larger functional roles within proteins."

* Sarah Krause of Harford County, Maryland, who earned her bachelor's degree in chemistry at Towson University and is pursuing her doctorate in organic chemistry at UD in Donald Watson's research group.

The focus of her research is chemical synthesis and catalysis.

* Andrew Kuznicki of Boston, Massachusetts, who is majoring in chemistry.

His research has been in the inorganic chemistry lab of Joel Rosenthal, associate professor of chemistry and biochemistry.

* Peter Sariano of Collegeville, Pennsylvania, an honors degree candidate who is majoring in biomedical engineering and plans to pursue research in tissue engineering.

"Biomedical research is the foundation for medical discovery. Research drives our understanding of disease and allows us to develop treatments to address unmet clinical needs."

* Hannah Wastyk of Palmyra, Pennsylvania, a du Pont Scholar and honors degree candidate majoring in biochemistry with a minor in biochemical engineering.

"What excites me most about research on human disease is that the body is a system more perfect than any we could possibly engineer. Our immune system is the most complex line of defense we possess, and treating diseases through regulation of its already existing cellular processes to control aberrant signaling is a technique that holds almost unlimited possibilities.

"The concept of growth has always been a passion I continually strive for. Research, both in practice and in mindset, perfectly embodies this endless cycle of growth through the creation of knowledge starting with basic research and applying it to solve real-world problems through engineering."

* Kathryn Wheeler of Boone, North Carolina, a du Pont Scholar and honors degree candidate who is earning her bachelor's degree in environmental science and will pursue a doctoral degree at Boston University's Department of Earth and the Environment.

"I am interested in how climate change is altering forest phenology (seasonality) and how the timing of the seasons affects the forest ecosystem and global ecosystems. Specifically, at Boston University I will be working on a project that uses ecosystem forecasting to identify the holes in our understanding of phenology and seasonal variation in carbon and energy transfers between the biosphere and atmosphere. With warmer global temperatures, the growing season is expected to be lengthened in many ecosystems. A longer growing season has the possibility of increasing the amount of carbon dioxide that trees take away from the atmosphere, which consequently would likely alleviate global climate change. In order to improve the accuracy of climate change predictions, it is necessary for us to better understand forest phenology and how it affects and is affected by climate change.

Research with Delphis Levia, professor of ecohydrology and chair of UD's Department of Geography, and doctoral student Janice Hudson introduced her to phenology.

"I became fascinated by the idea that something as seemingly simple as changing the timing of the seasons can have profound impacts on ecosystems. I became particularly interested in how phenology can then affect climate change through an ecosystems ecology course I took with Dr. Rodrigo Vargas [assistant professor of plant and soil sciences] this fall."

Hunter Bachman, mechanical engineering, an honors degree candidate, now at Duke University

Rabae Bounoua, psychology

Christopher Bresette, engineering, an honors degree candidate

Kamil Charubin, chemical engineering

Patrick Cronin, electrical and computer engineering

Nathan Hamilton, chemical engineering, an honors degree candidate

Alyssa Hull, chemistry and art conservation, a double honors degree recipient, now at Duke University

Joshua Lansford, chemical engineering

Charles McCutcheon, chemical engineering, now at the University of Minnesota

Bonnie McDevitt, environmental engineering, an honors degree recipient, now at Penn State University

Alexander Mitkas, chemical engineering

Samuel Modlin, neuroscience, now at San Diego State University Foundation

Lacey Perdue, bioengineering, an honors degree candidate

Jacob Wilmot, biology and neuroscience, an honors degree recipient, now at the University of California-Davis

A complete list of those offered the fellowship for 2017 is available on FastLane. For general information about the program, visit NSF's GRFP website.

Read this article:
NSF Graduate Research Fellowships | UDaily - University of Delaware - UDaily

March 28, 2017 by Layne Cameron Kristin Parent mapped the structure of the giant Samba virus with MSU's cryo-EM microscope, which is featured on the cover of the journal Viruses. Credit: Michigan State University

In a laboratory at Michigan State University, scientists took a DIY approach to build a retrofitted cryo-electron microscope that allowed them to map a giant Samba virus one of the world's largest viruses.

"If the common cold virus is scaled to the size of a ladder, then the giant Samba virus is bigger than the Washington Monument," said Kristin Parent, assistant professor of biochemistry and molecular biology and co-author of the paper featured on the cover of the journal Viruses. "Cryo-EM allowed us to map this virus' structure and observe the proteins it uses to enter, or attack, cells."

It seems counterintuitive that bigger organisms are harder to see, but they are when using cryo-electron microscopy. That's because these microscopes usually are used to look at thin specimens and can't decipher larger organisms to reveal their biological mechanisms. For thick samples, scientists see only dark gray or black blobs instead of seeing the molecular framework.

Cryo-EM allowed Parent's team to image the giant Samba virus and understand the structures that allow it to enter an amoeba. Once inside, Samba opens one of its capsid layers and releases its nucleocapsid which carries the genetic cargo that sparks an infection. While Samba isn't known to cause any diseases in humans, its cousin, the mimivirus, may be a culprit for causing some respiratory ailments in humans.

"If you scoop up a handful of water from Lake Michigan, you are literally holding more viruses than there are people on the planet," said Parent, who published the paper with Jason Schrad and Eric Young, MSU biochemistry and molecular biology graduate students. "While scientists can't study every virus on Earth, the insights we glean from viruses like the giant Samba can help us understand the mechanisms of other viruses in its family, how they thrive and how we can attack them."

As bacteria become more resistant to antibiotics, looking for new ways to fight diseases will continue to grow in importance. Parent's lab also studies how bacteria-infecting viruses enter cells using this method, which could potentially lead to new antibacterial treatments. Yet the world's best cryo-EM microscope costs more than $5 million. Limited by funds but not drive, Parent was able to upgrade an existing microscope at MSU to do cryo-EM one that is a tinkerer's dream.

This traditional transmission electron microscope was retrofitted with a cryostage, which keeps viruses frozen in liquid nitrogen while they're being studied. Parent and her team then added a Direct Electron DE-20 detector, a powerful camera the mighty microscope's piece de resistance.

Parent didn't invent cryo-EM, but establishing it on campus serves as a viable proof-of-concept for MSU, opening the door for many interdisciplinary partnerships. This cutting-edge microscopy has applications across many fields, from those addressing a single protein to others studying entire cells. Virtually anyone studying complex molecular machines can advance their work with this tool, Parent added.

Parent has earned an AAAS Marion Milligan Mason Award for Women in the Chemical Sciences. This award, her paper in Viruses and being the co-author who performed cryo-EM work in a recent Nature Communications paper, lays the groundwork to some day have a more advanced cryo-EM microscope housed at MSU to be able to perform high-resolution structural studies.

"We've done quite a bit with our limited resources, but we're primed to do more," Parent said. "I think MSU could serve as a cryo-EM center and to increase the prevalence of this technology in the Midwest and beyond."

As one example, scientists from Universidade Federal de Minas Gerais (Brazil) and Universidade Federal do Rio de Janeiro (Brazil) also contributed to this study and benefitted from the technology MSU has to offer.

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Scientist maps giant virus - Phys.Org