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X-ORIGINAL-URL:https://asrc.gc.cuny.edu
X-WR-CALDESC:Events for The Advanced Science Research Center
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DTSTART;TZID=America/New_York:20251008T120000
DTEND;TZID=America/New_York:20251008T130000
DTSTAMP:20260521T120452
CREATED:20250821T165608Z
LAST-MODIFIED:20251006T150758Z
UID:10001511-1759924800-1759928400@asrc.gc.cuny.edu
SUMMARY:Fall '25 Biochem Seminar: Associate Professor Kimberly Reynolds
DESCRIPTION:Mapping and modeling the impact of protein biochemical variation on growth rate phenotype \nIndividual proteins can be expressed\, purified\, and exquisitely characterized in terms of their biochemical and biophysical parameters in vitro. However\, the quantitative relationship between these parameters and complex phenotypes like growth remains mysterious. For example\, what values of protein abundance\, thermal stability (ΔGfold) and catalytic activity (kcat\, Km) must an enzyme attain to sustain metabolic pathway flux and support cell growth? In many cases\, we are missing even orders-of-magnitude level bounds on these fundamental biochemical parameters — we do not have a sense of which protein properties must be precisely tuned and which are robust to variation. To address this knowledge gap\, my lab seeks to quantify the intracellular constraints on protein abundance\, activity\, regulation\, and ultimately sequence. We then use this information to engineer new protein systems and build mathematical models relating protein activity and sequence to phenotype. In this talk\, I will first discuss our recent study of how variation in the activity of one enzyme constrains the biochemical parameters and sequence of another. Using a combination of deep mutational scanning and mathematical modeling we showed that inter-enzyme biochemical coupling can strongly reshape an enzyme’s sensitivity to mutation. Then\, I will introduce a CRISPR-interference based strategy for quantitatively mapping the relationship between protein expression level and cell growth. We used these high throughput measurements to train an interpretable machine learning model that predicts growth rate given combinatorial variation in gene expression and environment. Together these data lay a foundation for defining the biochemical “design specifications” of metabolic pathways and cell systems. \nPlease use this link to access Zoom. \n\n\n\nFor any questions\, please contact Hyacinth Camillieri at hcamillieri@gc.cuny.edu.
URL:https://asrc.gc.cuny.edu/event/fall-25-biochem-seminar-assistant-professor-kimberly-reynolds/
LOCATION:ASRC Auditorium\, 85 St. Nicholas Terrace\, New York\, NY\, 10031\, United States
CATEGORIES:Structural Biology
ATTACH;FMTTYPE=application/pdf:https://asrc.gc.cuny.edu/wp-content/uploads/media/event/fall-25-biochem-seminar-assistant-professor-kimberly-reynolds/20251008_reynolds_flyer.pdf
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DTSTART;TZID=America/New_York:20251015T120000
DTEND;TZID=America/New_York:20251015T130000
DTSTAMP:20260521T120452
CREATED:20250821T165706Z
LAST-MODIFIED:20251010T144301Z
UID:10001512-1760529600-1760533200@asrc.gc.cuny.edu
SUMMARY:Fall '25 Biochem Seminar: Professor Michael Sattler
DESCRIPTION:Dynamic RNA-protein interactions in A-to-I editing and biomolecular condensates in non- coding RNA pathways \nWe employ integrative structural biology\, combining solution NMR with complementary techniques and molecular dynamics to study the dynamics of RNAs and RNA-protein interactions in RNA processing pathways\, including alternative splicing regulation and non- coding RNA pathways. The structural understanding is a starting point to identify small molecule inhibitors that modulate these pathways for novel therapeutic approaches. Starting from a brief outline of our work and approaches in splicing regulation\, two studies will be presented: (1) We discovered extensive dynamics associated with A-to-I hyper-edited dsRNAs\, which exhibit unique conformational features. These features are specifically associated with hyper-editing and are specifically recognized by inosine binding proteins such as Endonuclease V. (2) We are dissecting the molecular principles of biomolecular condensates that are implicated in the separation of small non-coding RNA pathways in Drososphila\, combining NMR\, biophysical techniques and cell microscopy. \nPlease use this link to access Zoom. \n\n\n\nFor any questions\, contact Hyacinth Camillieri at hcamillieri@gc.cuny.edu.
URL:https://asrc.gc.cuny.edu/event/fall-25-biochem-seminar-professor-michael-sattler/
LOCATION:ASRC Auditorium\, 85 St. Nicholas Terrace\, New York\, NY\, 10031\, United States
CATEGORIES:Structural Biology
ATTACH;FMTTYPE=application/pdf:https://asrc.gc.cuny.edu/wp-content/uploads/media/event/fall-25-biochem-seminar-professor-michael-sattler/20251015_sattler_flyer.pdf
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BEGIN:VEVENT
DTSTART;TZID=America/New_York:20251028T163000
DTEND;TZID=America/New_York:20251028T183000
DTSTAMP:20260521T120452
CREATED:20251007T001942Z
LAST-MODIFIED:20251007T001942Z
UID:10001531-1761669000-1761676200@asrc.gc.cuny.edu
SUMMARY:Family Science Night
DESCRIPTION:Don’t be afraid of science; join us for Family Science Night at the CUNY ASRC. We will have fun science activities for all ages\, braaiiinns\, crystals\, lasers\, and more! Plus\, a tour with trick-or-treating on every floor. See you on October 28 from 4:30 p.m. to 6:30 p.m.\n\nRSVP today at https://bit.ly/4pWKPrD\n\n\nDownload and share the flyer
URL:https://asrc.gc.cuny.edu/event/family-science-night/
LOCATION:Advanced Science Research Center (ASRC)\, 85 St. Nicholas Terrace\, New York\, NY\, 10031\, United States
CATEGORIES:Environmental Sciences,Nanoscience,Neuroscience,Photonics,Structural Biology
ATTACH;FMTTYPE=image/jpeg:https://asrc.gc.cuny.edu/wp-content/uploads/media/event/family-science-night/TAYB8667_1280x720.jpg
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BEGIN:VEVENT
DTSTART;TZID=America/New_York:20251029T120000
DTEND;TZID=America/New_York:20251029T130000
DTSTAMP:20260521T120452
CREATED:20250821T165751Z
LAST-MODIFIED:20251017T170415Z
UID:10001513-1761739200-1761742800@asrc.gc.cuny.edu
SUMMARY:Fall '25 Biochem Seminar: Professor Lillian Chong
DESCRIPTION:Catching Rare Events in Action with Weighted Ensemble MD \nRare biological and chemical events often lie beyond the reach of conventional simulations. The weighted ensemble (WE) path sampling strategy overcomes this barrier\, extending accessible timescales by orders of magnitude while maintaining rigorous kinetics. By directly simulating pathways and stepwise rates\, WE reveals molecular mechanisms in unprecedented detail. In this talk\, I will highlight recent advances in WE methodology and showcase applications to hidden protein states and chemical reactions. \nPlease use this link to access Zoom. \n\n\n\nFor any questions\, please contact Hyacinth Camillieri at hcamillieri@gc.cuny.edu.
URL:https://asrc.gc.cuny.edu/event/fall-25-biochem-seminar-professor-lillian-chong/
LOCATION:ASRC Auditorium\, 85 St. Nicholas Terrace\, New York\, NY\, 10031\, United States
CATEGORIES:Structural Biology
ATTACH;FMTTYPE=application/pdf:https://asrc.gc.cuny.edu/wp-content/uploads/media/event/fall-25-biochem-seminar-professor-lillian-chong/20251026_chong_flyer.pdf
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