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DTSTART;TZID=America/New_York:20230208T120000
DTEND;TZID=America/New_York:20230208T130000
DTSTAMP:20260919T035613
CREATED:20221024T200628Z
LAST-MODIFIED:20230131T182954Z
UID:10001325-1675857600-1675861200@asrc.gc.cuny.edu
SUMMARY:ASRC-CCNY Seminar Series in Biochemistry\, Biophysics and Biodesign: Pilar Cossio\, Flatiron Institute
DESCRIPTION:In this weekly seminar series\, Pilar Cossio\, Research Scientist and Project Leader for the Structural & Molecular Biophysics Center for Computational Mathematics\, Flatiron Institute\, New York\, NY\, will present a one-hour talk titled: \n Free energies from cryoEM particles \nAbstract   Cryo-electron microscopy (cryo-EM) is an experimental technique that measures single-particle projections of biomolecules. Although single-particle cryo-EM is widely used for 3D reconstruction\, it has the potential to provide information about a biomolecule’s conformational variability and provide quantitative measurements of probability distributions. However\, cryo-EM images are challenging to analyze due to their low signal-to-noise ratio. To address these issues\, we developed mathematical methods to infer free-energy profiles and their uncertainties from cryo-EM raw images. \nThis seminar will be presented in the ASRC Auditorium and broadcast via Zoom\, with snacks and refreshments to start at 11:30am in the cafe. \nTo join these ongoing events via Zoom\, please use the meeting info below: \nMeeting ID:  968 3104 2138\nPasscode:  ASRC-CDI \nFor more information about this hybrid event\, please contact: \nHyacinth Camillieri \nhcamillieri@gc.cuny.edu
URL:https://asrc.gc.cuny.edu/event/asrc-ccny-seminar-series-in-biochemistry-biophysics-and-biodesign-pilar-cossio-flatiron-institute/
LOCATION:ASRC Auditorium & Cafe\, 85 St. Nicholas Terrace\, New York\, NY\, 10031\, United States
CATEGORIES:Structural Biology
ATTACH;FMTTYPE=image/png:https://asrc.gc.cuny.edu/wp-content/uploads/media/event/asrc-ccny-seminar-series-in-biochemistry-biophysics-and-biodesign-pilar-cossio-flatiron-institute/Spring-SBI-Seminar-website-image.png
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DTSTART;TZID=America/New_York:20230215T120000
DTEND;TZID=America/New_York:20230215T130000
DTSTAMP:20260919T035613
CREATED:20221024T201922Z
LAST-MODIFIED:20230209T175627Z
UID:10001326-1676462400-1676466000@asrc.gc.cuny.edu
SUMMARY:ASRC-CCNY Seminar Series in Biochemistry\, Biophysics and Biodesign: Tanja Mittag\, St. Jude Children's Research Hospital
DESCRIPTION:In this weekly seminar series\, Tanja Mittag\, Member of the Structural Biology Department Faculty\, St. Jude Children’s Research Hospital\, Memphis\, TN\, will present a one-hour talk titled: \nConcepts in phase separation – from sequence-encoded driving forces to material properties \nABSTRACT Phase transitions underlie cellularcompartmentalization and mediate fundamental biologicalprocesses. How the driving force for phase separation is encodedin the protein sequence is therefore an important question. Here\,we use biophysical experiments\, theory\, and simulations togenerate a conceptual stickers-and-spacers framework tounderstand phase behavior of intrinsically disordered prion-likelow-complexity domains (PLCDs) of RNA-binding proteins.Stickers form non-covalent inter-and intramolecular crosslinks\,whereas spacers enable or suppress the formation of thesecrosslinks. We have previously shown that aromatic residues arethe stickers in the PLCD of hnRNPA1. Here\, we demonstrate thatsticker residues mediate networking and spacer residues influencephase separation through their effective solvation volume. Ouranalytical and coarse-grained models accurately predict PLCDphase behavior. Based on the resulting stickers-and-spacersmodel\, we can think of condensates as network fluids. We areextending our stickers-and-spacers framework to understandmaterial properties of condensates and how their aging processes\,which have been linked to neurodegenerative diseases\, areinfluenced by network structure and interfaces. \nThis seminar will be presented in the ASRC Auditorium and broadcast via Zoom\, with snacks and refreshments to start at 11:30am in the cafe. \nTo join these ongoing events via Zoom\, please use the link below: \nMeeting ID: 968 3104 2138 \nPasscode: ASRC-CDI \nFor more information about this hybrid event please contact: \nHyacinth Camillieri \nhcamillieri@gc.cuny.edu
URL:https://asrc.gc.cuny.edu/event/asrc-ccny-seminar-series-in-biochemistry-biophysics-and-biodesign-tanja-mittag-st-jude-childrens-research-hospital/
LOCATION:ASRC Auditorium & Cafe\, 85 St. Nicholas Terrace\, New York\, NY\, 10031\, United States
CATEGORIES:Structural Biology
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END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20230222T120000
DTEND;TZID=America/New_York:20230222T130000
DTSTAMP:20260919T035613
CREATED:20221024T203924Z
LAST-MODIFIED:20230216T193608Z
UID:10001327-1677067200-1677070800@asrc.gc.cuny.edu
SUMMARY:ASRC-CCNY Seminar Series in Biochemistry\, Biophysics and Biodesign: Giovanna Ghirlanda\, Arizona State University
DESCRIPTION:In this weekly seminar series\, Giovanna Ghirlanda\, professor at the School of Molecular Sciences\, Arizona State University\, Tempe\, AZ\, will be presenting a one-hour talk titled: \nArtificial metalloproteins by design \nABSTRACT Hybrid metalloproteins incorporating organometallic active sites not found in nature within a protein scaffold are emerging as a viable avenue to catalyze a wide range of reactions\, with applications ranging from synthetic organic chemistry to sustainable fuel production. This approach is particularly appealing when coupled with light as a source of energy to drive the synthesis of clean energy sources. We have designed artificial enzymes capable of producing molecular hydrogen and reducing carbon dioxide to carbon monoxide and formate under irradiation with UV-vis light and in the presence of photosensitizers. The active site in these designs is either anchored to protein scaffolds using noncanonical amino acids\, or obtained by swapping heme for cobalt protoporphyrin IX in natural and designed heme-binding proteins. Intriguingly\, these constructs are active in aerobic conditions. We found that incorporation in a protein scaffold increases activity by 10-20 folds compared to the isolated organometallic complex. Transient spectroscopy analysis demonstrates that this effect correlates with increased lifetime of the catalytically active redox state. Current work examines the activity of these constructs within bacterial cells. \nThis seminar will be presented in the ASRC Auditorium and broadcast via Zoom\, with snacks and refreshments to start at 11:30am. \nTo join these ongoing events via Zoom\, please use the link below: \nMeeting ID: 968 3104 2138\nPasscode: ASRC-CDI \nFor more information about this hybrid event please contact: \nHyacinth Camillieri \nhcamillieri@gc.cuny.edu
URL:https://asrc.gc.cuny.edu/event/asrc-ccny-seminar-series-in-biochemistry-biophysics-and-biodesign-giovanna-ghirlanda-arizona-state-university/
LOCATION:ASRC Auditorium & Cafe\, 85 St. Nicholas Terrace\, New York\, NY\, 10031\, United States
CATEGORIES:Structural Biology
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