Category Archives: Biochemistry

Biochemistry

USM Chemistry (Biochemistry Emphasis) Degree Earns ASBMB Reaccreditation – The University of Southern Mississippi

Wed, 01/31/2024 - 01:21pm | By: Ivonne Kawas

The University of Southern Mississippis (USM) B.S. degree in Chemistry (Biochemistry emphasis) has earned reaccreditation by the leading agency in the field of life sciences the American Society for Biochemistry and Molecular Biology (ASBMB).

This accreditation was obtained for the first time in 2017. Obtaining ASBMB accreditation, a national outcomes-based evaluation, ensures programs in the field meet the highest standards of academic excellence. USMs chemistry degree program is housed in the School of Mathematics and Natural Sciences (MANS),

Accreditation by ASBMB is a testament to the quality and content of our biochemistry curriculum, as well as to the knowledge and skills learned by our students as they begin to seek careers or further their studies at the graduate or professional levels, said Dr. Chris Winstead, dean of the College of Arts and Sciences. I appreciate the effort of the faculty in seeking this accreditation. This shows their dedication to providing the best preparation possible for our Southern Miss students, an education that is well-aligned with national standards and prepares them for their next steps.

Dr. Vijay Rangachari, professor of chemistry and biochemistry, emphasizes one of the direct accreditation benefits for students.

ASBMB accreditation inherently enhances the value of the students degree, allowing them to include on their resume that they graduated from an ASBMB-accredited program. Furthermore, upon degree completion, they can demonstrate competitiveness on a national scale by obtaining ASBMB certification.

Dr. Rangachari also highlights one of the strengths of the program, integral to both student success and ASBMB accreditation: the hands-on research opportunities provided in the laboratory.

To meet accreditation requirements, the curricula must include over 400 hours of hands-on laboratory experience. Therefore, students get an advantage in advancing their careers.

Students like Landon Lee, a native of Hattiesburg, Miss. who is pursuing the biochemistry emphasis, actively participate in cutting-edge research projects in the lab, alongside graduate students and faculty mentors.

Joining a research lab has significantly enriched my educational experience, as Ive been able to acquire skills related to academic research, project management, and creative thinking, said Lee. With the support and guidance from both the graduate students in my lab and Dr. Rangachari, my faculty mentor, it has become more than just a platform for applying classroom concepts; it has provided me a community that fosters my personal and academic development.

After completing his bachelors degree, Lee plans to further his studies: As I complete my degree, I intend to pursue a Ph.D. in neuroscience. My coursework has undoubtedly laid a strong foundation in physics, chemistry, and mathematics, enabling me to demonstrate key strengths as I strive toward this goal.

Dr. Theofanis Kitsopoulos, director in the School of MANS, reflects on the programs successful and highly valued alumni base, as it opens doors to diverse industries.

Our curriculum is carefully crafted to equip students not only with a strong theoretical foundation but also with practical skills highly valued in the job market, said Dr. Kitsopoulos. Several of our alumni choose to pursue advanced degrees in prestigious graduate programs in medical, dental, pharmaceutical, and other professional schools. They go on to succeed in diverse industries such as research and development, healthcare, environmental consulting, forensic science, and entrepreneurship. Some thrive as quality control and analytical chemists, while others pursue fulfilling paths as middle and high school science and chemistry teachers.

Learn more about the B.S. degree in Chemistry (Biochemistry emphasis).

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USM Chemistry (Biochemistry Emphasis) Degree Earns ASBMB Reaccreditation - The University of Southern Mississippi

Biochemistry

AI generates proteins with exceptional binding strength – ASBMB Today

A new studyin Nature reports an AI-driven advance in biotechnology with implications for drug development, disease detection, and environmental monitoring. Scientists at the Institute for Protein Design at the University of Washington School of Medicine used software to create protein molecules that bind with exceptionally high affinity and specificity to a variety of challenging biomarkers, including human hormones. Notably, the scientists achieved the highest interaction strength ever reported between a computer-generated biomolecule and its target.

Ian Haydon, UW Medicine Institute for Protein Design

Susana Vasquez-Torres in a UW Medicine Institute for Protein Design laboratory, where she is working to develop new proteins with high-binding affinity and specificity to a variety of challenging biomarkers.

Senior author David Baker, professor of biochemistry at UW Medicine, Howard Hughes Medical Institute investigator, and recipient of the 2023 Frontiers of Knowledge Award in Biology and Biomedicine, emphasized the potential impact: "The ability to generate novel proteins with such high binding affinity and specificity opens up a world of possibilities, from new disease treatments to advanced diagnostics."

Ian Haydon/UW Medicine Institute for Protein Design

A new protein designed using deep-learning methods. In this case, RFdiffusion generates a binding protein.

The team, led by Baker Lab members Susana Vazquez-Torres, Preetham Venkatesh, and Phil Leung, set out to create proteins that could bind to glucagon, neuropeptide Y, parathyroid hormone, and other helical peptide targets. Such molecules, crucial in biological systems, are especially difficult for drugs and diagnostic tools to recognize because they often lack stable molecular structures. Antibodies can be used to detect some of these medically relevant targets but are often costly to produce and have limited shelf lives.

"There are many diseases that are difficult to treat today simply because it is so challenging to detect certain molecules in the body. As tools for diagnosis, designed proteins may offer a more cost-effective alternative to antibodies," explained Venkatesh.

The study introduces a novel protein design approach that uses advanced deep-learning methods. The researchers present a new way of using RFdiffusion, a generative model for creating new protein shapes, in conjunction with the sequence-design tool ProteinMPNN. Developed in the Baker Lab, these programs allow scientists to create functional proteins more efficiently than ever before. By combining these tools in new ways, the team generated binding proteins by using limited target information, such as a peptide's amino acid sequence alone. The broad implications of this "build to fit" approach suggest a new era in biotechnology in which AI-generated proteins can be used to detect complex molecules relevant to human health and the environment.

Ian Haydon/UW Medicine Institute for Protein Design

An AI-designed protein in detail from the UW Medicine Institute for Protein Design.

"We're witnessing an exciting era in protein design, where advanced artificial intelligence tools, like the ones featured in our study, are accelerating the improvement of protein activity. This breakthrough is set to redefine the landscape of biotechnology," noted Vazquez-Torres.

In collaboration with the Joseph Rogers Lab at the University of Copenhagen and the Andrew Hoofnagle Lab at UW Medicine, the team conducted laboratory tests to validate their biodesign methods. Mass spectrometry was used to detect designed proteins that bind to low-concentration peptides in human serum, thereby demonstrating the potential for sensitive and accurate disease diagnostics. Additionally, the proteins were found to retain their target binding abilities despite harsh conditions including high heat, a crucial attribute for real-world application. Further showcasing the method's potential, the researchers integrated a high-affinity parathyroid hormone binder into a biosensor system and achieved a 21-fold increase in bioluminescence signal in samples that contained the target hormone. This integration into a diagnostic device highlights the immediate practical applications of AI-generated proteins.

The study, which illustrates the confluence of biotechnology and artificial intelligence and sets a new precedent in both fields, appears in Nature with the title De novo design of high-affinity binders of bioactive helical peptides.

(This article was produced by the University of Washington School of Medicine/UW Medicine.)

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AI generates proteins with exceptional binding strength - ASBMB Today

Biochemistry

A safe place where biochemistry is valued – ASBMB Today

I earned my B.S. and Ph.D. from Peking University, China, and received postdoctoral training at Yale University. I am now an assistant professor in the biochemistry and structural biology department at the Greehey Childrens Cancer Research Institute at the University of Texas Health Science Center at San Antonio.

Xuemei Song

Weixing Zhao enjoys the cultural richness and great Tex-Mex food in San Antonio.

Breast cancer genes 1 and2, known as BRAC1/2, produceproteinsthat help repair damaged DNA, and it is well known that mutations in these genes can lead to cancer. My laboratory purifies full-length BRCA1/2 complexes and reconstitutes their biochemical reactions to investigate the BRCA1/2 tumor suppressor networks in related biological processes and the molecular mechanisms underlying their pathogenic mutations. We aim to provide the foundation and impetus for developing new therapeutic regimens.

Four years ago, I decided to relocate to San Antonio to kickstart my career, a choice heavily influenced by the collegial atmosphere at UTHSCSA. What stood out most was the administration's genuine appreciation for foundational biochemical studies.

San Antonio has been a joy to live in, with its seamless mix of tradition and modernity. The city boasts a rich heritage influenced by Mexican, Spanish and

Native American cultures, not to mention its delectable food. I particularly love the authentic Tex-Mex dishes, the vibrant markets of El Mercado and the tranquil strolls along the River Walk. San Antonio is a truly enchanting place. Most importantly, its friendly vibe and affordable cost of living make me feel secure and confident in raising a family here.

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A safe place where biochemistry is valued - ASBMB Today

Biochemistry

Chair (W3) of Biochemistry job with TECHNISCHE UNIVERSITAT … – Times Higher Education

TUD Dresden University of Technology, as a University of Excellence, is one of the leading and most dynamic research institutions in the country. Founded in 1828, today it is a globally oriented, regionally anchored top university as it focuses on the grand challenges of the 21st century. It develops innovative solutions for the world's most pressing issues. In research and academic programs, the university unites the natural and engineering sciences with the humanities, social sciences and medicine. This wide range of disciplines is a special feature, facilitating interdisciplinarity and transfer of science to society. As a modern employer, it offers attractive working conditions to all employees in teaching, research, technology and administration. The goal is to promote and develop their individual abilities while empowering everyone to reach their full potential. TUD embodies a university culture that is characterized by cosmopolitanism, mutual appreciation, thriving innovation and active participation. For TUD diversity is an essential feature and a quality criterion of an excellent university. Accordingly, we welcome all applicants who would like to commit themselves, their achievements and productivity to the success of the whole institution.

At the Faculty of Chemistry and Food Chemistry, the

Chair (W3) of Biochemistry

is to be filled as of October 1, 2024.

You (m/f/x) will represent the entire field of biochemistry both in teaching and research. In teaching, you will represent the subject of biochemistry across all study programs in the Faculty of Chemistry and Food Chemistry as well as in the subsidiary subject training of associated or English-language study programs. Your willingness to actively participate in interdisciplinary projects (e.g. CRCs, graduate schools), to cooperate with the non-university research institutions located in Dresden as well as to actively participate in academic self-administration is expressly desired.

We require successful scientific activities with international visibility in the field of biochemistry. Your research in experimental biochemistry should ideally focus on the elucidation of biosynthetic pathways in secondary metabolism as a basis for the sustainable production of bioactive compounds and thus be distinct from the other chairs with a biochemical focus at TU Dresden, which are predominantly oriented to molecular genetics or medicine, and complement them in terms of content. Extensive experience in teaching biochemistry, special didactic skills and success in acquiring third-party funding are also expected. Applicants must fulfil the employment qualification requirements of 59 of the Act on the Autonomy of Institutions of Higher Education in the Free State of Saxony (SchsHSFG).

For further questions, please contact the chairman of the appointment committee, Prof. Michael Hellwig (Tel. +49 351 463 32006; email: michael.hellwig@tu-dresden.de)

TUD strives to employ more women in academia and research. We therefore expressly encourage women to apply. The University is a certified family-friendly university and offers a Dual Career Service. We welcome applications from candidates with disabilities. If multiple candidates prove to be equally qualified, those with disabilities or with equivalent status pursuant to the German Social Code IX (SGB IX) will receive priority for employment. If you have any questions about these topics, please contact the Equal Opportunities Officer of the Faculty of Chemistry and Food Chemistry (Ms. Dr. Anke Matura, +49 351 463 35505, anke.matura@tu-dresden.de) or Representative of Employees with Disabilities (Mr. Roberto Lemmrich, +49 351 463 33175).

We look forward to receiving your application by December 11, 2023 (time stamp on the email server or the stamped arrival date of the University Central Mail Service of TUD applies).

Please attach the following documents to your letter of application: curriculum vitae in table form, a synopsis of your academic career, a list of academic publications, a list of courses, results of teaching evaluations covering the last three years, a research and teaching concept, offprints of your five most important publications, summary of your third-party funding, and a copy of the certificate of your highest academic degree.

We kindly ask you to submit your application by email. Please use the SecureMail Portal of TUD (https://securemail.tu-dresden.de) and send your documents in a single PDF document to: dekanat.chemie@tu-dresden.de. If you are applying by regular mail, please also attach your application documents in electronic form (CD or USB thumb drive) and send them to: TU Dresden, Dekan der Fakultt Chemie und Lebensmittelchemie, Herrn Prof. Dr. Stefan Kaskel, Helmholtzstr. 10, 01069 Dresden, Germany.

Reference to data protection: Your data protection rights, the purpose for which your data will be processed, as well as further information about data protection is available to you on the website: https://tu-dresden.de/karriere/datenschutzhinweis.

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Chair (W3) of Biochemistry job with TECHNISCHE UNIVERSITAT ... - Times Higher Education

Biochemistry

The Biochemistry of Muscle Contraction – Discovery Institute

Photo credit: Edgar Chaparro, via Unsplash.

In an article yesterday, I gave a short overview of the arrangement and structure of muscles. Here, I will describe the biochemistry of muscle contraction. Readers may find it slightly easier to follow the discussion that follows by first viewing this short animation, which describes the sliding filament model of muscle contraction.

I previously noted that muscles contain thousands of cylindrical cells called muscle fibers, or myocytes. The motor neuron terminates at the muscle fibers neuromuscular junction. The tip of the motor neuron is known as the axon terminal, and it contains sacs of acetylcholine, an important neurotransmitter involved in muscle contraction. The muscle fiber also has a membrane called the sarcolemma, containing acetylcholine receptor sites, in addition to an inactivator called cholinesterase. The small space between the sarcolemma and axon terminal is called the synapse, or synaptic cleft.

The muscle fiber contains thousands of individual contracting units known as sarcomeres. These are organized end-to-end in cylinders known as myofibrils. In the center of the sarcomere are thick filaments comprised predominantly of the protein myosin, and thin filaments containing actin can be found at the ends, attached to the end boundaries of the sarcomere (known as the Z discs) by the protein titin. The structure of the muscle fiber is shown in the figure below:

Muscle contraction is driven by two contractile proteins myosin and actin. Each myosin molecule consists of a long tail and a globular head. Myosin heads have ATPase activity, which allows them to hydrolyze ATP to generate energy for muscle contraction. Myosin heads also have binding sites for actin and ATP. Actin has binding sites for myosin heads. However, these binding sites are typically covered by two inhibitory proteins known as tropomyosin and troponin when the muscle is relaxed. These inhibitory proteins prevent the sliding of myosin and actin during relaxation of the muscle fiber.

The sarcomeres are surrounded by the sarcoplasmic reticulum (the muscular equivalent of the endoplasmic reticulum), which serves as a reservoir of calcium ions (Ca2+). As we shall see, Ca2+ions are required for muscle contraction.

When a muscle fiber is in a state of relaxation, the sarcolemma has a resting potential, or is said to be polarized. This refers to the difference in electrical charges between the inside and outside. When the sarcolemma is polarized, there is a positive charge outside relative to the negatively charged inside. There is a greater concentration of sodium ions (Na+) outside the cell and a greater concentration of potassium ions (K+) and negative ions inside the cell.

Because of the concentration gradient, the Na+ions tend to diffuse into the cell and the K+ions tend to diffuse outside. These are actively transported back out and in respectively by the sodium and potassium pumps, which depend upon ATP to maintain polarization and muscle relaxation until a change is stimulated by a nerve impulse.

The first step in muscle contraction is the arrival of a nerve impulse at the axon terminal, stimulating the release of the neurotransmitter acetylcholine. The acetylcholine diffuses across the synapse and binds to acetylcholine receptors on the sarcolemma. This renders the sarcolemma extremely permeable to Na+ions, which rapidly enter the cell. This reverses the charges such that there is now a positive charge on the inside of the sarcolemma relative to the outside. This charge reversal is known as depolarization.

Inward folds on the sarcolemma known as transverse tubules (or, T tubules) carry this electrical impulse (referred to as an action potential) to the interior of the muscle cell. Depolarization triggers the release of Ca2+ions from the sarcoplasmic reticulum. These bind to the troponin-tropomyosin complex, moving it away from the actin filaments.

With the binding sites on actin now available, actin can be bound by the myosin heads, forming cross-bridges. Once the cross-bridges are formed, the myosin heads pivot, pulling the thin filaments towards the center of the sarcomere. This action is called the power stroke and is powered by the energy released when ATP is hydrolyzed. After the power stroke, the myosin heads require ATP to detach from actin. ATP is hydrolyzed into ADP and inorganic phosphate, which energizes the myosin head for the next cycle.

The cycle of cross-bridge formation, power stroke, ATP hydrolysis, and detachment repeats as long as calcium ions are present and ATP is available. This results in the shortening of the sarcomere and, collectively, the entire muscle fiber. This leads to muscle contraction. The force generated by many muscle fibers contracting in unison allows for body movement. The sliding filament model is graphically summarized in the figure below:

Muscle relaxation occurs when the electrical stimulation ceases resulting in the ionic concentrations inside and outside the cell returning to their resting state. To restore the resting-membrane potential, the Na+and K+pumps actively transport sodium ions out of the cell while bringing potassium ions back into the cell. This returns the membrane potential to its polarized, negative resting state, typically around -90mV for muscle cells. Repolarization results in the myosin heads releasing their grip on actin, and calcium ions are actively transported back into the sarcoplasmic reticulum, causing muscle relaxation.

As should be apparent from the forgoing discussion, muscle contraction which we so easily take for granted is an incredibly complex and elegant process, involving incredible engineering and design. The process of muscle contraction and relaxation requires the coordinated action of actin, myosin, troponin, tropomyosin, acetyl choline, ion channels, and much more. To contend that the phenomenon of muscle contraction arose through a blind and undirected process, one tiny Darwinian step after the other, seems to me to strain credulity.

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The Biochemistry of Muscle Contraction - Discovery Institute

Biochemistry

Department of Biochemistry and Molecular Biology chair and … – University of Iowa Health Care

The fourth semifinalist candidate for the position of chair and department executive officer of the Department of Biochemistry and Molecular Biology will deliver a seminar this week to present their qualifications, share their vision for the department, and answer employee questions.

Peter Kaiser, PhD, chair and professor of biological chemistry at the University of California, Irvine, will present his seminar titled, Exploring Ubiquitin/Metabolite Signaling and Attempts to Restore Tumor Suppression in Cancer, from 10:30 to 11:30 a.m. Thursday, Oct. 26, in the Urmila Sahai Auditorium in MERF. A reception will immediately follow in the skywalk in PBDB.

UI Health Care employees are welcome and encouraged to join the candidate seminar in person. You may forward any questions in advance for the candidate Q&A sessions to sasha-alexander@uiowa.edu.

The fourth semifinalist candidate for the position of chair and department executive officer of the Department of Biochemistry and Molecular Biology will deliver a seminar this week to present their qualifications, share their vision for the department, and answer employee questions.

Peter Kaiser, PhD, chair and professor of biological chemistry at the University of California, Irvine, will present his seminar titled, Exploring Ubiquitin/Metabolite Signaling and Attempts to Restore Tumor Suppression in Cancer, from 10:30 to 11:30 a.m. Thursday, Oct. 26, in the Urmila Sahai Auditorium in MERF. A reception will immediately follow in the skywalk in PBDB.

UI Health Care employees are welcome and encouraged to join the candidate seminar in person. You may forward any questions in advance for the candidate Q&A sessions to sasha-alexander@uiowa.edu.

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Department of Biochemistry and Molecular Biology chair and ... - University of Iowa Health Care

Biochemistry

Two decorated Brandeis faculty awarded National Medal of Science … – Brandeis University

By Lawrence Goodman October 24, 2023

Pioneering neuroscientist Eve Marder69 and Professor of Biochemistry and Chemistry Emeritus Gregory Petsko have each received the National Medal of Science, the highest recognition the nation bestows on scientists and engineers.

The awards were announced by President Biden at a ceremony at the White House on October 24.

Both of these remarkable individuals have conducted significant scientific research that has had a major impact on repairing the world, and both have trained generations of Brandeisians to go out and do the same, said Brandeis President Ron Liebowitz, who was at the White House to attend the awards ceremony. Eve and Greg have dedicated much of their careers to our university, and for that, I am deeply grateful.

Marder, the Victor and Gwendolyn Beinfield Professor of Neuroscience and a University Professor, was honored for her visionary application of theoretical and experimental approaches to understanding neural circuits; and her inspirational advocacy of basic science, according to a press release from National Science and Technology Medals Foundation (NSTMF).

Currently at Harvard Medical School and Brigham and Womens Hospital in Boston, Petsko, who is a member of Brandeis Board of Trustees, was recognized for advancing our understanding of neurodegenerative diseases like ALS, Alzheimers, and Parkinsons, the NSTMF press release said.

His role in founding structural enzymology, along with his commitment to educating the public about brain health, have empowered people around the world and raised the ambitions of our nation regarding aging with dignity, the release added.

Marder joined the Brandeis faculty as an assistant professor in 1978 and remained on thefaculty ever since.

She has revolutionized scientists understanding of neuronal circuit operation, including how neuromodulators, chemicals that alter the activity of neurons, affect an organisms behavior. She studies a small network of 30 neurons in the nervous system of lobsters and crabs, which she realized early in her career could serve as a model for understanding the basic properties common to all brains.

She has received numerous prestigious prizes, including the Gruber Prize, the Kavli Prize, and the National Academy of Sciences Award. She served as president of the Society for Neuroscience as well as on the working group for President Obamas BRAIN Initiative. She is a member of the National Academy of Sciences, the American Academy of Arts & Sciences, and the Institute of Medicine.

Last month, she received the 2023 Pearl Meister Greengard Prize, which recognizes outstanding women scientists.

Petskos research concerns the three-dimensional structures of proteins and their biochemical functions. His public lectures on the aging of the population and its implications for human health have attracted a wide audience, including a TED Talk that has been viewed over 900,000 times.

He has collaborated extensively with Professor of Biochemistry and Chemistry EmeritaDagmar Ringe.

His awards include the Sidhu Award and the Martin J. Buerger Award, both from the American Crystallographic Association, the Pfizer Award in Enzyme Chemistry from the American Chemical Society, the Lynen Medal, and the Max Planck Research Award.

He is a Fellow of the American Association for the Advancement of Science and has been elected to the National Academy of Sciences, the National Academy of Medicine, the American Academy of Arts and Sciences, and the American Philosophical Society.

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Two decorated Brandeis faculty awarded National Medal of Science ... - Brandeis University

Biochemistry

Research Assistant / Associate (Department of Biochemistry) job … – Times Higher Education

Job Description

The National University of Singapore invites applications forResearch Assistant/Research Associate for Industrializing non-viral precision engineered mesenchymal stem cell biofactoriesin the Department ofDepartment of Biochemistry, Yong Loo Lin School of Medicine. Appointments will be made on a1 yearcontract basis in the first instance, with the possibility of extension.

Purpose of the post

Our laboratory has developed a non-viral based gene delivery platform (Nucleic Acids Res. 2017 Apr 7; 45(6): e38). The Research Assistant/Research Associate (RA) will be responsible to, and work closely with, the Principal Investigator and study team members to develop gene based applications R&D and clinical application. Our team in the midst of preparation for a phase I clinical trial for recurrent Glioblastoma patients.

Main Duties and Responsibilities

The Research Assistant will work with the project lead (current Post doc) to carry out research in the area of gene modification of mammalian cells, including designing and running experiments, recording, analyzing and writing up the results (as part of a research team).

The RA will be able to:

Qualifications

The requirements are:

Application

Remuneration will be commensurate with the candidates qualifications and experience. Informal enquiries are welcome and should be made toHo Yoon Khei, at bchhyk@nus.edu.sg.

Formal application: Please submit your application, indicating current/expected salary, supported by a detailed CV (including personal particulars, academic and employment history, complete list of publications/oral presentations and full contacts of three (3) referees to this job portal.

We regret that only shortlisted candidates will be notified.

More Information

Location: Kent Ridge Campus Organization: Yong Loo Lin School of Medicine Department: Biochemistry Employee Referral Eligible: No Job requisition ID: 18422

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Research Assistant / Associate (Department of Biochemistry) job ... - Times Higher Education

Biochemistry

ASBMB weighs in on policy changes for dual-use research – ASBMB Today

The American Society for Biochemistry and Molecular Biology sent feedback on Oct. 16 to the White House Office of Science and Technology Policy about its proposed changes to policy frameworks for dual-use research of concern and potential pandemic pathogen care.

The ASBMB recommended that OSTP:

Create tools to aid scientists in determining which research requires additional scrutiny,

create measurable outcomes for redefining potential pandemic pathogens, and

solicit feedback from the scientific community.

Ann West is the associate vice president for research and development and a professor at the University of Oklahoma. She leads the ASBMB Public Affairs Advisory Committee. We are advocating for more unified and clear guidance from the various federal agencies and a multilayer approach to understanding the research communitys concerns prior to implementation, West said.

Various types of life sciences research are classified as dual-use because they can be used to help or harm humanity. Federal and institutional dual-use policies and potential pandemic pathogen care policies cover 15 agents with potential biosafety and biosecurity risks.

The National Science Advisory Board for Biosecurity, a federal advisory committee, released recommendations in March to address biosecurity and dual-use research concerns. Following the boards recommendations and proposed policy changes, OSTP released a request for information in September with three broad goals:

Assess the merger of existing policies into one harmonized policy,

expand the scope of pathogens and toxins with the potential to impact humans, and

determine ways to strengthen the implementation of oversight throughout the research cycle.

The NSABB proposes merging existing dual-use and potential pathogen policies into one. This would significantly reduce the high administrative burden placed on researchers and academic institutions conducting this type of research. According to the National Science Foundation, principal investigators of federally sponsored projects spend 42% of their time on administrative tasks.

The ASBMB encouraged OSTP to solicit feedback from the scientific community to prevent an increase in administrative burden on scientists and their institutional biosafety committees and to prepare the scientific community for the changes.

The NSABB proposes revising the scope of pathogens and toxins requiring review to (1) expand beyond the current 15 select agents and pathogens, (2) redefine potentially pandemic pathogens to include moderately or highly transmissible and/or virulent and (3) remove blanket exclusions for select agents and toxins.

The White House Office of Science and Technology Policy isrevising oversight policies for infectious disease-related research.

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ASBMB Public Affairs Advisory Committee member Matthew Koci is a professor of immunology, virology and hostpathogen interactions at North Carolina State University. The challenge with these kinds of policies is they tend to exist in black-and-white lists, but Mother Nature works exclusively in shades of gray, he said.

Members of the scientific community have raised concerns that OSTP is overreaching. The authors of an editorial in the Journal of Virology in February warned that abundant unnecessary review could significantly slow down science.

The United States Government Accountability Office has expressed concerns about the vague standards in defining pandemic pathogens in current policies, saying that vaccine and surveillance research could be impeded by removing blanket exemptions for agents and toxins.

The ASBMB recommended OSTP:

Create tools to aid scientists in determining which agent, toxin or pathogen requires additional scrutiny and the biosafety level required,

create clearer definitions and measurable thresholds for defining potentially pandemic pathogens, and

involve the scientific community in revising the blanket exclusions with careful consideration of annual updates for seasonal influenza and SARS-CoV-2 vaccines.

The NSABB also recommends the inclusion of in silico (computer-generated) models into the harmonized policy to guard against the use of computers to design new or dangerous pathogens. The ASBMB recommended OSTP engage with community stakeholders and in silico research model experts to determine if this research poses a risk and to determine the best course of action.

The proposed revision to the definition of potentially pandemic pathogens states that scientists must determine if their research is likely to pose a severe threat to public health, the capacity of public health systems, or national security. Scientists do not have the appropriate information or expertise to make this type of determination. The ASBMB urged OSTP to create an external panel or board that defines and determines threats to national security. This will also give scientists some protection from undue public scrutiny.

The ASBMB acknowledged heightened concern about biosafety and biosecurity. However, the society urged OSTP to continue engaging the scientific community to minimize negative consequences relating to vaccine and surveillance research.

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ASBMB weighs in on policy changes for dual-use research - ASBMB Today

Biochemistry

In the Locker Room with Katie Austin, Mia Brito, and Alaina Di Dio … – The Oberlin Review

Austin, Brito, and Di Dio pose for media day.

Katie Austin, Mia Brito, and Alaina Di Dio are fourth-years on the softball team in addition to being captains and housemates. Austin is a Chemistry and Biochemistry major from San Diego, Brito is a History major from Covina, CA, and Di Dio is a Psychology major from Whitmore Lake, MI.

Since softball is a spring sport, they do not participate in games in the fall except for Fall Ball, one day when the team can play up to three games. On Oct. 7, the team hosted Ursuline College, an NCAA Division II school, and lost 64.

We played a DII [team], but we were definitely able to hold our own, which was great, Brito said. We lost a few players from last year, so its taken us a while to see where all the pieces are going to be for this year. Especially after play day, we have a much clearer idea of how our defense is going to shape up, and its looking really good.

Throughout the fall the team is allotted a set number of practices, which start in early September. After these, the team then transitions to captains practices for the rest of the fall, led by Austin, Brito, and Di Dio. In addition, they lift two to three times a week.

The three housemates have all played softball for many years. Austin has been playing since elementary school.

It was the first sport I ever played and I just stuck with it because I like pitching so much, Austin said. [I] essentially [have] control on the mound and we just get to be outside with our friends. Its a good environment and it teaches you a lot. Ive learned so much about dedication and teamwork from travel ball and then playing in college, and it builds a really strong community.

Brito has been playing softball since she was four years old. She hasnt stopped playing because her mom never got the opportunity to continue playing after high school.

I really like it, but I mostly play because my mom didnt get to, Brito said. She had my brother when she was 17, [so] she had to quit. So, I keep playing for her.

Di Dio credits softball as her break from school, which motivated her to keep playing at Oberlin.

In high school and now, its a time to get away from academics and responsibilities, Di Dio said. Its like structured hanging-out time with your friends; its your favorite people and you get to see them every day. Our team is so close-knit.

In their house, the fourth-years have a cherished cone, a softball tradition. Each year, the softball fourth-years pass on a giant megaphone cone to the next group of fourth-years, with each graduating class signing the interior. Maria Roussos, OC 18, came back during homecoming and noticed the megaphone cone sitting in their living room.

She goes, I cannot believe you guys still have this cone, Di Dio said. And were like, What? Shes like, I started this when I was in school, when I was a [first-year]. One of her [fourth-years] gave it to her. When youre a [fourth-year], you sign the cone under the cone, theres a list of names from all these years past. She came and saw it in our house and shes like, I am so glad someone still has it. I thought itd be thrown away right now. But I like that you guys are keeping the tradition forward. You have to give it to the next house.

Outside of softball, the three are constantly busy with other extracurricular activities, which the team is incredibly supportive of. Over the summer, Brito had the opportunity to study in Japan through the Luce Initiative on Asian Studies and the Environment Grant as an East Asian Studies minor. When she did her LIASE presentation at the beginning of the school year, the team came and watched her present. When Di Dio presented at the Undergraduate Research Symposium last year, she received similar support from her teammates and coaches who came to her presentation.

Since her second year at Oberlin, Brito has worked at the Multicultural Resource Center and as a manager at the Dionysus Disco. Over the last year and a half, she has been working with 15 different minority student groups on an archive for minority student groups on campus. She has gotten the school to approve a digital database, which will be uploaded to the Oberlin College Library server, and a physical archive, which will be in Wilder Hall. After Oberlin, she plans to take a gap year on campus to continue working on this project. Later, she plans to go into information science and archiving with a focus on social justice, library science, and information access.

Theres not many schools that are doing that, Brito said. Im very excited.

Di Dio is a peer tutor for Psychology and Statistics classes as well as a PRSM trainer on campus. She has been in multiple labs and assisted Visiting Assistant Professor of Politics Adam J. Howat in formulating a study investigating political identity and affective polarization. She currently does research at the Michigan State University Twin Registry, where shes mainly focused on studying the etiology and development of externalizing behavior, specifically antisocial behavior. She presented her research in Spain at the annual meeting of the Behavior Genetics Association. Shes currently applying to Ph.D. programs in clinical science and psychology, where she hopes to continue her work or go into the field of behavioral genetics.

Austin does research in the Ryno Lab in the Biochemistry department, looking at changes in the transcriptome of arabinose-treated E. coli. This summer, she participated in a nuclear and radiochemistry summer school program at San Jose State University, where she learned about the basics of nuclear chemistry and visited the Livermore National Laboratory and the Lawrence Berkeley National Laboratory. Now, shes looking at graduate schools for radiochemistry or biochemistry.

When asked about advice she would give to her first-year self, Austin was nostalgic about her time here.

Just enjoy the things that Oberlin has to offer, because its going by so quickly, Austin said. Its over already, and we have to cherish these last moments, like going to Long Island Night.

Di Dio believes that ones first-year and fourth-year selves are very different.

A lot changes between first year and fourth year, Di Dio said. You think you might have it figured out, but you dont roll with the changes.

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In the Locker Room with Katie Austin, Mia Brito, and Alaina Di Dio ... - The Oberlin Review