In the News
UMass Amherst Chemistry participates in the ACS Bridge Program which aims to diversify the graduate student population in the chemical sciences. The mentorship program, part of the NSF INCLUDES Alliance: Inclusive Graduate Education Network (IGEN), provides additional pathways for Black, Latino, and Indigenous students to receive doctoral degrees.
Prospective students are considered by all of the 22 participating institutions by submitting one application.
Prof. Michael Knapp, ACS Bridge Program leader for UMass Amherst Chemistry, commented on the success of the program, “I think we’ve all worked with people where they really don’t need or don’t want a lot of hand-holding. But making sure that the trampoline is there when you’re on the high wire is really important so that if you fall off, you can bounce back.”
You might not be on-campus or in a classroom, but you are not alone! We are here to help you be successful in your remote learning courses.
Preparing your Mind & Space to Learn. We’ve all heard the quote by Benjamin Franklin “By failing to prepare, you are preparing to fail.” Explore strategies and tools to assist you in preparing for success. Topics include: Mindset Matters, Developing a Growth Mindset A Set-up for Success, and My Learning Environment My Remote Learning Checklist.
Quick links to tools to help you get started: Mindset Matters, Reframing my Challenges, My Learning Environment, and My Remote Learning Checklist
Make your Learning Meaningful. Strive for higher levels of learning and create your learning routines. Strategies and tools to assist you in meaningful learning. Topics include: Higher Levels of Learning, A Learning Routine for Success, and My Study Cycle. Quick links to tools to help you get started: Levels of Learning and The Study Cycle.
Master the Content. As you strive for higher levels of learning, it is important to have a toolbox of strategies to reply on. Your approach to learning will vary by course and change as you progress in your major. Expand your learning toolbox with the following resources on academic success strategies: Concept Maps, Active Reading Strategies, Note Taking Strategies, Study & Review Strategies, and Explore how your academic habits may impact test taking. You are not alone. Connect with resources to support your content mastery. Success Toolkit Series, Learning Resource Center, Writing Center, and talk to your Academic Advisor about college/major specific academic support services.
Make the Most of your Time. Effectively utilizing your time is a life long skill. Learning to prioritize assignments, studying and other commitments is a personal journey. Explore these tips to discuss tools and strategies that may help you make the most of your time. Topics include: Finding a Routine & Tools, Time Management, and Tools Managing Procrastination. Quick link to tools to help you get started: Student Success Planner, Managing your Procrastination, and Where does my time go?
The operational posture of the UMass Amherst campus is currently at "Guarded." For more information, go to www.umass.edu/spring.
The campus’s strategic focus is on advancing students’ academic progress toward degree completion while providing a campus environment that meets federal and state health and safety protocols for mitigating COVID-19. Guided by these principles, the university has determined that in-person, face-to-face instruction for undergraduate and graduate students will be offered on campus this spring in certain classes, labs and studios identified as requiring in-person instruction.
Timely information regarding various aspects of our spring plan can be found at umass.edu/spring, and the administration will also keep you updated via email and other communication channels.
In the weeks and months ahead, the campus will continue to monitor the progress of the pandemic, and should worsening conditions warrant re-evaluation of our plan, we will act accordingly to ensure that the health and wellbeing of our community remains paramount
UMass Chemist Eric Strieter and his lab group have discovered how an enzyme known as UCH37 regulates a cell’s waste management system, a result they found “incredibly surprising.”
Strieter says, “It took us eight years to figure it out, and I’m very proud of this work. We had to develop a lot of new methods and tools to understand what this enzyme is doing.”
As he explains, a very large protease called a proteasome is responsible for degrading the vast majority of proteins in a cell; it may be made up of as many as 40 proteins. It has been known for more than 20 years that UCH37 is one of the regulatory enzymes that associates with the proteasome, he adds, “but no one understood what it was doing.” It turns out that the crux of the whole process, he adds, is how complicated modifications in a small protein called ubiquitin can be.
Writing this week in Molecular Cell, he and first author and Ph.D. candidate Kirandeep Deol, who led and conducted the experiments, with co-authors Sean Crowe, Jiale Du, Heather Bisbee and Robert Guenette, discuss how they answered the question. The work was supported by the NIH’s National Institute of General Medical Sciences.
This advance could eventually lead to a new cancer treatment, Strieter says, because cancer cells need the proteasome to grow and proliferate.
Project leader and chemistry professor Dhandapani “DV” Venkataraman, is one of five researchers from a campus group that has been selected to receive a one-year, $100,000 grant from the National Science Foundation’s “10 Big Ideas for Future NSF Investments” series to conduct a series of national workshops to identify research challenges associated with transitioning to an equitable and sustainable energy system.
The grant is the second this year from the National Science Foundation (NSF) to researchers at UMass for a similar purpose, evidence of a growing worldwide interest in developing sustainable energy systems that consider and even prioritize the resources and needs of all communities.
“A transition toward a less carbon-intensive energy system is underway globally,” Venkataraman points out. “The challenge is to envision how the energy system might evolve in a way that is consistent with resources and needs.”
Further, he explains, “When we are thinking about the emerging energy technologies landscape, we need to incorporate equity as an intrinsic design component. This requires energy scientists, equity scholars and other stakeholders who normally work independently to come together and identify the priorities and needs.”
Hardy Wins Teaching Award
Jeanne Hardy has won the Northeastern Association of Graduate Schools Graduate Faculty Teaching Award (Doctoral level). The Northeastern Association of Graduate Schools includes member institutions in 11 states, Washington, D.C. and 6 Canadian provinces. The award recognizes Prof. Hardy’s excellence and creativity in teaching graduate students, as well as her innovation in graduate curriculum development and implementation. Prof. Hardy has provided industrially-relevant and hands-on training to graduate students in Chemistry and several life sciences and engineering majors via courses she developed such as Drug Design and Frontiers in Biotechnology and through co-founding and directing the interdisciplinary Biotechnology Training Program, which trains students in biotechnology via courses and industrial internships.
Finalist for ACS President Has Ties to UMass Chemistry
Professor Mary K. Carroll of Union College is one of two finalists in the fall election for 2021 president-elect of the American Chemical Society, the world’s largest scientific society with 152,000 members in more than 140 countries. Carroll has local ties to the UMass Chemistry department, having been a postdoctoral researcher with Professor Julian Tyson (1991-92).
Carroll has co-directed the Union College Aerogel Laboratory, a productive interdisciplinary research group. To date, more than 150 undergraduate STEM majors, several high-school students and faculty colleagues from Union and other institutions have participated in the group’s research in the fabrication, characterization and applications of aerogel materials.
She is active in the American Chemical Society (ACS) and since 1998 has served as a councilor of the Eastern New York ACS section. At the national level, she currently serves on the ACS Committee on Science. Based on her contributions to science and service to the ACS, Mary Carroll was selected for recognition as a member of the class of 2016 ACS Fellows.
Research Corporation for Science Advancement (RCSA) has named Michelle Farkas, chemistry, one of 13 new Fellows for its Scialog: Chemical Machinery of the Cell (CMC) initiative.
Co-sponsored by RCSA and the Gordon and Betty Moore Foundation, Scialog: Chemical Machinery of the Cell aims to catalyze breakthroughs in our understanding of chemical processes in the living cell that will lead to a new era of advancement in cell biology.
The new early-career researchers, together with Fellows selected in the previous two years, will convene virtually Oct. 9, for a half-day meeting. The final in-person CMC conference is scheduled for Oct. 7 – 10, 2021, in Tucson, Ariz.
“It’s terrific to have 13 new Fellows join this outstanding community of rising stars,” said senior program director Richard Wiener. Scialog is short for “science + dialog.” As part of each multiyear initiative, a diverse and inclusive cohort of Fellows is selected from multiple disciplines and institutions across the U.S. and Canada to maximize creative thinking and innovative ideas.
At each conference, participants form multidisciplinary teams to design research projects, which they pitch to leading scientists who have facilitated discussions throughout the meeting. A committee of these facilitators then recommends seed funding to catalyze the most promising of those team projects.
“Even though we can’t meet in person in 2020, we’re excited to keep the community engaged virtually to think of new, potentially high-impact ideas to advance our understanding of cellular processes,” Wiener added. “That momentum will carry us into our final CMC conference and a final round of funding next year.”
A chemist and kinesiologist got on a bus, but this isn’t the set-up to a joke. Instead, kinesiologist and lead author Ned Debold and chemist Dhandapani Venkataraman, “DV,” began talking on their bus commute to the University of Massachusetts Amherst and discovered their mutual interest in how energy is converted from one form to another – for Debold, in muscle tissue and for DV, in solar cells.
An alternative energy source to replace the body’s usual one, a molecule called adenosine triphosphate (ATP, could control muscle activity, and might lead to new muscle spasm-calming treatments in cerebral palsy, for example, or activate or enhance skeletal muscle function in MS, ALS and chronic heart failure.
The usual approach to seeking a new compound is to systematically test each one among millions until one seems worth followup – the classic “needle in a haystack” says DV. “At one point I suggested to Ned, ‘Why don’t we build the needle ourselves instead?’ That started us on this interesting project that put together people who would otherwise never work together.” Computational chemist, Jianhan Chen, was invited to model interactions between the molecules DV was making and the myosin molecules Debold was using to test them.
Chen explains, “We did computer modeling because experimentally it is difficult to know how myosin might be using the molecules DV was synthesizing. We can use computer simulation to provide a detailed picture at the molecular level to understand why these compounds might have certain effects. This can provide insight into not only how myosin interacts with the current set of compounds, but also it can provide a roadmap for DV to use to design new compounds that are even more effective at altering myosin function.”
This month, the researchers report in the Biophysical Journal that they have made a series of synthetic compounds to serve as alternative energy sources for the muscle protein myosin, and that myosin can use this new energy source to generate force and velocity. Mike Woodward from the Debold lab is the first author of their paper and Xiaorong Liu from the Chen lab performed the computer simulation.
The next stage for the trio will be to map the process at various points in myosin’s biochemical cycle.
In the molecular-level world of ion channels – passageways through membranes that carry signals in a cell’s environment and allow it to respond – researchers have debated about the role of a small piece of the channel called a linker, says computational biophysicist Jianhan Chen.
The linker communicates between the pore and its environment-sensing apparatus, and knowing its function – whether it’s inert or plays an active sensing role – has been unclear. But it might lead to a new target for drugs and treatment in conditions such as hypertension, autism, epilepsy, stroke and asthma, he adds. Now, Chen and colleagues at Washington University report in eLife that their experiments have revealed “the first direct example of how non-specific membrane interactions of a covalent linker can regulate the activation of a biological ion channel.”
Specifically, Chen and co-first authors Mahdieh Yazdani and Zhiguang Jia at UMass Chemistry, with co-first author Guohui Zhang, Jingyi Shi and Jianmin Cui at Washington University, studied a pore called the large-conductance potassium (BK) channel. It is important in muscle and neuron function and is controlled by calcium concentration via a calcium-sensing domain. It is also controlled by electrical potential through a voltage-sensing domain. Either way, it opens and closes like a gate – “a really common architecture in transmembrane receptors and channels,” Chen says.
During the first 48-hour Sciathon hosted by the Council for the Nobel Laureate Meetings, Steve Acquah, the UMass Amherst Libraries Digital Media Lab coordinator and associate research professor of chemistry, worked as part of a team (Group Clifton) to develop a science news verification tool, authentiSci. The Clifton group became finalists at the end of June and were recently awarded second place in the category of ‘Lindau Guidelines’ and a shared prize of 1,000 Euros. AuthentiSci can be accessed through the website authentisci.com and will primarily be used through a Google Chrome Extension, which is now available at the Chrome Web Store. The extension is one of the first of its kind that gives scientists the ability to score science news stories, providing a measure of confidence for the reader.
The section of the Lindau Guidelines had the highest amount of competition, with 23 out of the 48 groups working on Lindau Guideline based projects. The other project sections focused on the topics Communicating Climate Change and Capitalism After Corona.
The extension was produced in response to the Lindau Guidelines introduced by Elizabeth Blackburn during the 68th Lindau Nobel Laureate Meeting held in Lindau, Germany, in June 2018. To use the extension, scientists would authenticate through their ORCID account, insert a URL from a news story, and follow the prompts to evaluate the story on authentisci.com. With the extension now available, people from around the world will be able to see verified news stories.
Acquah produced a video during the 48-hour event highlighting the work of the team.
Alzheimer’s disease has been intensely studied for decades, too much is still not known about molecular processes in the brain that cause it. Chemistry Professor Jianhan Chen says new insights from analytic theory and molecular simulation techniques offer a better understanding of amyloid fibril growth and brain pathology.
As senior author Chen notes, the “amyloid hypothesis” was promising – amyloid protein fibrils are a central feature in Alzheimer’s, Parkinson’s disease and other neurodegenerative diseases. “But the process is really difficult to study,” he says. Chen and first author Zhiguang Jia, a research scientist in Chen’s computational biophysics lab, explored how building-block peptides form fibrils. “We are really proud of this work because, to the best of our knowledge, for the first time we have described the comprehensive process of how fibril growth can happen. We illustrate that the effects of disease-causing mutations often arise from the cumulative effects of many small perturbations. A comprehensive description is absolutely critical to generate reliable and testable hypothesis,” he adds. Details of their multi-scale approach with many atomistic simulations are in Proceedings of the National Academy of Sciences.