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DTSTART;TZID=America/Chicago:20190405T153000
DTEND;TZID=America/Chicago:20190405T163000
DTSTAMP:20190401T184311Z
CREATED:20190319T180816Z
LAST-MODIFIED:20190401T184311Z
UID:10381446-1554478200-1554481800@uwm.edu
SUMMARY:Physics Colloquium - Aaron Viets
DESCRIPTION:Aaron Viets\, PhD Candidate\, University of Wisconsin-Milwaukee \nOptimizing Advanced LIGO’s Scientific Output with Fast\, Accurate\, Clean Calibration \nFast\, accurate calibration of Advanced LIGO data is an essential part of gravitational-wave astronomy\, necessary for prompt electromagnetic follow-up of gravitational-wave events and reliable estimation of source parameters.    \nI will discuss methods used in both low and high latency to produce the calibrated strain signal h(t).   I will highlight recent improvements that have been made to improve the calibration process during and after the second observing run.  These include the application of frequency-dependent corrections to the calibration using adaptive filters\, reduction in calibration latency\, and the subtraction of excess noise from h(t) in low latency. \nEvent flyer available here.
URL:https://uwm.edu/physics/event/pqviets040519/
LOCATION:Lapham 160\, 3209 N. Maryland Ave.\, Milwaukee\, WI\, 53211\, United States
CATEGORIES:Physics Colloquia
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GEO:43.0757204;-87.8840564
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BEGIN:VEVENT
DTSTART;TZID=America/Chicago:20190412T153000
DTEND;TZID=America/Chicago:20190412T163000
DTSTAMP:20190409T140024Z
CREATED:20190319T180816Z
LAST-MODIFIED:20190409T140024Z
UID:10381448-1555083000-1555086600@uwm.edu
SUMMARY:Physics Colloquium - Victor Muñoz
DESCRIPTION:Victor Muñoz\, University of California-Merced \nLessons About Biomolecular Rate Theory from Ultrafast Kinetics and Single-Molecule Spectroscopy of Fast-Folding Proteins \nNatural proteins fold and unfold with rates that define their biological properties and vary vastly from protein to protein.  Understanding how these rates are determined is essential to decipher the mechanisms of protein folding\, but is also a convenient system to explore the fundamental aspects of biomolecular rate theory.  Protein (un)folding rates are described as diffusion on a free energy surface obtained by projecting the protein-solvent hyper-dimensional phase space (or folding energy landscape) onto one or few order parameters that capture the reaction’s progress.  Such description often reduces to Kramers rate theory\, in which the rates depend on the free energy barrier separating the native and unfolded states and a prefactor term that sets the timescale for crossing such barrier or folding speed limit.  A pervasive problem in the field has been the impossibility to extricate these two factors from experimentally measured folding and unfolding rates.  However\, recent work in the biophysical characterization of ultrafast protein folding and technical advances in single-molecule fluorescence and force spectroscopy are providing first direct glimpses of the (un)folding transition paths (the reactive barrier crossing events) undertaken by individual protein molecules and how they connect to the free energy barrier.   \nIn my talk\, I will review some of our recent results in this area that shed new light onto the mechanisms of protein folding and provide useful tests of the applicability of Kramers rate theory to biomolecular processes. \nEvent flyer downloadable here
URL:https://uwm.edu/physics/event/pqmunoz041219/
LOCATION:Lapham 160\, 3209 N. Maryland Ave.\, Milwaukee\, WI\, 53211\, United States
CATEGORIES:Physics Colloquia
X-TRIBE-STATUS:
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X-APPLE-STRUCTURED-LOCATION;VALUE=URI;X-ADDRESS=Lapham 160 3209 N. Maryland Ave. Milwaukee WI 53211 United States;X-APPLE-RADIUS=500;X-TITLE=3209 N. Maryland Ave.:geo:-87.8840564,43.0757204
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BEGIN:VEVENT
DTSTART;TZID=America/Chicago:20190419T153000
DTEND;TZID=America/Chicago:20190419T163000
DTSTAMP:20190415T202512Z
CREATED:20190319T180816Z
LAST-MODIFIED:20190415T202512Z
UID:10381450-1555687800-1555691400@uwm.edu
SUMMARY:Physics Colloquium - Piotr E. Marszalek
DESCRIPTION:Piotr E. Marszalek\, Duke University \nNanomechanics of Biopolymers Beyond Their Entropic Elasticity Regime \nCompared to other single-molecule techniques\, AFM-based force spectroscopy uses stiff force transducers and it may apply large stretching forces to molecules\, enabling their structural modifications and capturing high energy conformations that cannot be examined by (for example) X-ray crystallography or NMR. In my talk\, I will present our AFM stretching and relaxation studies\, supported by computer simulations of individual molecules of DNA and proteins. \nWhile differences between the molecular elasticity of single-stranded and double-stranded DNA were directly determined by optical tweezers as early as 1996\, our AFM studies 10 years later captured unexpected similarities between the nanomechanical behavior of single- and double-stranded DNA when they share the same canonical structures\, suggesting a common overstretching mechanism. AFM measurements of large multi-domain proteins\, combined with coarse-grained Steered Molecular Dynamics simulations\, revealed complex unfolding and refolding reactions that do not follow a simple two-state model typically observed for smaller proteins. Taken together\, these studies contribute to elucidating the (still not fully understood) mechanism of folding large proteins in vivo and may be useful in examining the mechanism by which large proteins avoid pathways to unproductive and disease-prone misfolded states. \nEvent flyer available here
URL:https://uwm.edu/physics/event/pqmarszalek041919/
LOCATION:Lapham 160\, 3209 N. Maryland Ave.\, Milwaukee\, WI\, 53211\, United States
CATEGORIES:Physics Colloquia
X-TRIBE-STATUS:
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X-APPLE-STRUCTURED-LOCATION;VALUE=URI;X-ADDRESS=Lapham 160 3209 N. Maryland Ave. Milwaukee WI 53211 United States;X-APPLE-RADIUS=500;X-TITLE=3209 N. Maryland Ave.:geo:-87.8840564,43.0757204
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BEGIN:VEVENT
DTSTART;TZID=America/Chicago:20190426T153000
DTEND;TZID=America/Chicago:20190426T163000
DTSTAMP:20190424T125147Z
CREATED:20190319T180816Z
LAST-MODIFIED:20190424T125147Z
UID:10381454-1556292600-1556296200@uwm.edu
SUMMARY:Physics Colloquium - Naomi McClure-Griffiths
DESCRIPTION:Professor Naomi McClure-Griffiths\, Professor at the Research School of Astronomy & Astrophysics in the College of Science – Australian National University \nThe Milky Way and Magellanic Clouds as Laboratories for Understanding the Evolution of Galaxies \nGalaxies are not closed box systems.  Their evolution is impacted by gas accreted via inflow\, gas lost from the disk via large-scale outflows and gas circulations via the halo.  Many simulations of galaxy formation and evolution have highlighted the importance of feedback in reproducing the observable Universe.  In this talk\, I will present an overview of observational evidence for outflows within the Milky Way and Magellanic Clouds.  Superbubbles\, formed from the stellar winds and supernovae of up to hundreds of massive stars\, these large-scale features dominate the observed structure of neutral hydrogen within the many galaxies.  Superbubbles that grow as large as the gas layer can burst to create galactic outflows\, which can circulate hot\, enriched gas within a galaxy’s halo and out of its gravitational potential to enrich the surrounding intergalactic medium.  The Milky Way and Magellanic system have many spectacular examples of gaseous outflows\, which we are able to study with physical resolution unmatched anywhere else in the Universe.    In this talk I will give an overview of how superbubbles develop and break out to form galactic outflows.   I will describe how atomic hydrogen emission data of the nearest galactic systems is helping us to understand how galaxies evolve. \nEvent flyer available here.
URL:https://uwm.edu/physics/event/pqmcclure-griffiths042619/
LOCATION:Lapham 160\, 3209 N. Maryland Ave.\, Milwaukee\, WI\, 53211\, United States
CATEGORIES:Physics Colloquia
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