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X-WR-CALDESC:Events for The Advanced Science Research Center
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DTSTART;TZID=America/New_York:20201007T120000
DTEND;TZID=America/New_York:20201007T130000
DTSTAMP:20260521T104032
CREATED:20201001T180524Z
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SUMMARY:Seminar in Biochemistry\, Biophysics & Biodesign: A. James Link\, Princeton University
DESCRIPTION:Speaker: A. James Link\, Professor of Chemical & Biological Engineering\, Princeton University \nTitle: Lasso Peptide Genome Mining for New Enzyme Discovery \nAbstract: Lasso peptides are a class of ribosomally synthesized and posttranslationally modified peptides (RiPPs) that are typified by a chiral rotaxane structure that resembles a slipknot. Lasso peptides exhibit a range of bioactivities including targeted antimicrobial activities. Our group pioneered genome mining for lasso peptides in 2012\, showing that gene clusters for these peptides are present in 2-3% of all sequenced prokaryotic genomes. This percentage has held true as the number of sequenced genomes has grown from ~3000 in 2011 to well over 200000 today. Because of the diversity in size and sequence\ninherent in lasso peptides\, the rediscovery rate of these natural products is low. In addition to uncovering lasso peptides with novel structures\, properties\, and activities\, searching genomes for lasso peptide gene clusters has led to the discovery of new enzymes\, two of which I will describe in this talk. The first\, lasso peptide isopeptidase\, is a lasso peptide catabolic enzyme that converts the slipknotted lasso structure into a linear peptide. This enzyme suggests a novel function for lasso peptides and also provides a glimpse into how enzymes cope with substrates that are subject to genetic drift. More recently\, we have characterized a new toxin-antitoxin pair that was embedded within a lasso peptide gene cluster. The toxin is a new example of an ADPribosyltransferase\, and it modifies an essential enzyme for nucleotide biosynthesis. Structural analysis of the toxin suggests a novel\, potentially ancient\, catalytic solution to the problem of ADPribosylation. \nFor more information about this seminar and about joining in online\, please contact Hyacinth Camillieri at hcamillieri@gc.cuny.edu
URL:https://asrc.gc.cuny.edu/event/seminar-in-biochemistry-biophysics-biodesign-a-james-link-princeton-university/
LOCATION:Online
CATEGORIES:Structural Biology
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DTSTART;TZID=America/New_York:20201014T120000
DTEND;TZID=America/New_York:20201014T130000
DTSTAMP:20260521T104032
CREATED:20201001T190414Z
LAST-MODIFIED:20201009T145842Z
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SUMMARY:Seminar in Biochemistry\, Biophysics & Biodesign: Janet Iwasa\, University of Utah
DESCRIPTION:Speaker: Janet Iwasa\, Assistant Professor\, Biochemistry Department\, University of Utah\, School of Medecine \nTitle: Animating Biology \nAbstract: Over the past decade\, there has been a significant increase in the use of 3D animation to depict molecular processes. Much of this growth has been made possible by recent advances in imaging technologies and methodologies. We have now accumulated diverse datasets that describe molecular structures\, dynamics\, functions\, interactions and localization with increasing clarity and confidence\, allowing researchers to construct detailed hypotheses or mental models of molecular processes that synthesize these data. As a molecular animator\, I use software from the entertainment industry to create animations that depict a specific molecular hypothesis. During this presentation\, I will share a number of insights drawn from over a decade of experience creating molecular animations with numerous research collaborators on diverse molecular topics. I will describe the workflow my group members and I have developed for creating a molecular animation and share some observations we have made on how the animation process can help researchers refine and explore their hypotheses. I will also demonstrate how 3D animation can be particularly beneficial for understanding and describing dynamic and complex molecular machines and large molecular assemblies within the context of the cell. Molecular animations have also made their way into the educational and public stages\, and have proven to be useful for engaging diverse audiences. Finally\, I will discuss the importance of broad scientific communication and describe various outreach projects we have undertaken. \nFor more information about this seminar and about joining in online\, please contact Hyacinth Camillieri at hcamillieri@gc.cuny.edu
URL:https://asrc.gc.cuny.edu/event/seminar-in-biochemistry-biophysics-biodesign-janet-iwasa-university-of-utah/
LOCATION:Online
CATEGORIES:Structural Biology
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20201016T130000
DTEND;TZID=America/New_York:20201016T140000
DTSTAMP:20260521T104032
CREATED:20200811T152430Z
LAST-MODIFIED:20201106T165501Z
UID:10001151-1602853200-1602856800@asrc.gc.cuny.edu
SUMMARY:Meet the Editor: Open Access Journals
DESCRIPTION:Meet the Editor: Open Access Journal Publication\nJoin us on October 16\, 2020 at 1 p.m. for a session with eLife Editor-In-Chief Michael Eisen and Nature Communications Editor-in-Chief Elisa De Ranieri\, where we’ll discuss considerations for publishing with open-access journals. \nBy doing away with paywalls\, open-access journals are endeavoring to democratize scientific learning and more quickly advance discovery. There are a growing number of these journals for scientists to consider when making decisions about research paper submission\, and they each have content\, protocol and a peer review process that are unique to their publishing missions. We’ll explore the ins and outs in this session with editors from two highly esteemed open-access journals. \nOur guests will cover: \n\nWhat their journals look for in research submissions\nThe nuances of writing for their publications\nThe peer review process\nAdditional opportunities\, such as becoming a reviewer or contributing other forms of editorial content\n\nThere will be opportunity for Q&A. \n\nThis event has passed. Watch the video recording below: \n \nCheck out the Graduate Center Science Communications Academy website where you can learn about our events and access science communications training tools.
URL:https://asrc.gc.cuny.edu/event/meet-the-editor-open-access-journals/
LOCATION:Online
CATEGORIES:Environmental Sciences,Nanoscience,Neuroscience,Photonics,Structural Biology
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BEGIN:VEVENT
DTSTART;TZID=America/New_York:20201021T120000
DTEND;TZID=America/New_York:20201021T130000
DTSTAMP:20260521T104032
CREATED:20201001T191138Z
LAST-MODIFIED:20201016T192937Z
UID:10001164-1603281600-1603285200@asrc.gc.cuny.edu
SUMMARY:Seminar in Biochemistry\, Biophysics & Biodesign: Frans Mulder\, Aarhus University
DESCRIPTION:Speaker: Frans Mulder\, Associate Professor\, Department of Chemistry\, Aarhus University \nTitle: Probing and predicting the behavior of intrinsically disordered proteins by integrating NMR spectroscopy and computation \nAbstract: I will focus on how we can utilize different NMR experimental observables to construct\, validate\, and improve models to understand protein behavior. I will discuss two topics: (1) NMR chemical shifts are exquisite probes of protein order and disorder\, and are recognized proxies of local structure. Deviations from ‘random coil chemical shifts’ can\, for example\, be used to detect structured regions or motifs in intrinsically disorder in proteins. We have used NMR chemical shifts to assess the quality and bias in current protein disorder predictors and provide a ranking of these. Subsequently we built an even better one. (2) Hydrogen exchange (HX) is a very powerful way to probe protein structure and to deduce local stability and (un)folding kinetics. The slowing down of HX rates is typically due to hydrogen bond formation upon folding\, although electrostatics also play a role. So far\, the latter contribution has only been regarded qualitatively. I will show how we efficiently compute the electric potential in the vicinity of an intrinsically disordered protein\, and how the thermodynamic concept of the electrochemical potential actually predicts the observed protection factors for the IDP alpha-synuclein. \nFor more information about this seminar and about joining in online\, please contact Hyacinth Camillieri at hcamillieri@gc.cuny.edu
URL:https://asrc.gc.cuny.edu/event/seminar-in-biochemistry-biophysics-biodesign-frans-mulder-aarhus-university/
LOCATION:Online
CATEGORIES:Structural Biology
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20201028T120000
DTEND;TZID=America/New_York:20201028T130000
DTSTAMP:20260521T104032
CREATED:20201001T191648Z
LAST-MODIFIED:20201022T181638Z
UID:10001165-1603886400-1603890000@asrc.gc.cuny.edu
SUMMARY:Seminar in Biochemistry\, Biophysics & Biodesign: Nobuhiko Tokuriki\, University of British Columbia
DESCRIPTION:Speaker: Nobuhiko Tokuriki\, Associate Professor\, Dept of Biochemistry & Molecular Biology\, University of British Columbia \nTitle: Dynamics and constraints of enzyme evolution \nAbstract: The wealth of distinct enzymatic functions found in nature is impressive and the on-going evolutionary divergence of enzymatic functions continues to generate new and efficient catalysts\, which can be seen through the recent emergence of enzymes able to degrade xenobiotics. How have these diverse enzyme functions evolved? Recreating such processes in the laboratory has been met with only moderate success. What are the factors that lead to suboptimal research outputs? I will present our recent efforts to enhance our understanding of evolution of enzyme functions within superfamilies. First\, I discuss about how seemingly unrelated catalytic activities observed in enzyme superfamilies are connected one to another through promiscuous enzymes. Second\, I will present a series of experimental evolution to evolve enzyme functions in the laboratory. I will discuss molecular basis underlying functional transitions\, e.g.\, molecular tinkering of active site residues and protein dynamics. Third\, I will describe constraints in enzyme evolution\, i.e.\, success of evolution can depend on initial genotypes. Finally\, I will discuss about how we could improve our ability to design and engineer novel proteins and enzymes in the laboratory. \nFor more information about this seminar and about joining in online\, please contact Hyacinth Camillieri at hcamillieri@gc.cuny.edu
URL:https://asrc.gc.cuny.edu/event/seminar-in-biochemistry-biophysics-biodesign-nobuhiko-tokuriki-university-of-british-columbia/
LOCATION:Online
CATEGORIES:Structural Biology
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