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X-WR-CALNAME:UCLA
X-ORIGINAL-URL:https://www.chemistry.ucla.edu
X-WR-CALDESC:Events for UCLA
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BEGIN:VTIMEZONE
TZID:America/Los_Angeles
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TZOFFSETFROM:-0800
TZOFFSETTO:-0700
TZNAME:PDT
DTSTART:20210314T100000
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TZOFFSETFROM:-0700
TZOFFSETTO:-0800
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DTSTART:20211107T090000
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BEGIN:VEVENT
DTSTART;TZID=America/Los_Angeles:20210111T160000
DTEND;TZID=America/Los_Angeles:20210111T160000
DTSTAMP:20260618T165946
CREATED:20210104T180919Z
LAST-MODIFIED:20210104T180919Z
UID:13406-1610380800-1610380800@www.chemistry.ucla.edu
SUMMARY:Chem 228: Michelle Y. Simmons\, Ph.D.
DESCRIPTION:“Engineering qubits in silicon with atomic precision”
URL:https://www.chemistry.ucla.edu/seminars/chem-228-michelle-y-simmons-phd/
CATEGORIES:Physical Chemistry Seminar,Seminars
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Los_Angeles:20210113T160000
DTEND;TZID=America/Los_Angeles:20210113T160000
DTSTAMP:20260618T165946
CREATED:20210105T015855Z
LAST-MODIFIED:20210105T015855Z
UID:13409-1610553600-1610553600@www.chemistry.ucla.edu
SUMMARY:Special Bio-Inorganic Chemistry Seminar
DESCRIPTION:“Tuning the Reactivity Landscape of Metalloenzymes: From Active Site Modifications to Long-range Dynamic Effects” \nAbstract: Metalloenzymes rely on transition metals within the protein scaffold to perform a wide variety of molecular transformations in biology. Synthetic models of metalloenzyme intermediates\, inspired by the enzyme active site and its secondary coordination sphere\, have provided systems for studying bond-forming/breaking events in well-controlled environments. However\, recent evidence has suggested that the dynamic nature of proteins is intimately linked to enzyme function and activity\, implying a reactivity landscape that is not only dependent on the ground state thermodynamics of the active site\, but also on the long-range protein motions that orient the active site for optimum catalysis. The first part of this presentation will focus on the synthesis and reactivity of high-valent metal-oxo and metal-hydroxo corroles and corrolazines as models for reactive intermediates in Cytochrome P450. The role of electronic structure\, peripheral ligand sterics\, and Lewis acid effects on oxygen atom transfer and hydroxyl radical rebound reactivities were evaluated in the context of how the active site microenvironment tunes the reactivity of heme enzymes. The second part of the presentation will focus on our current efforts on characterizing activity-related protein motions in the non-heme enzyme soybean lipoxygenase (SLO-1). SLO-1 utilizes a well-defined hydrogen tunneling mechanism that is intrinsically dependent on the motions of the protein scaffold. Collectively\, the findings from these research efforts have led to several fundamental insights regarding how reactivity is tuned from the active site and beyond\, providing a possible blueprint for the design of efficient catalysts for biological and industrial applications.
URL:https://www.chemistry.ucla.edu/seminars/special-bio-inorganic-chemistry-seminar-1/
CATEGORIES:Other,Seminars
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Los_Angeles:20210114T120000
DTEND;TZID=America/Los_Angeles:20210114T120000
DTSTAMP:20260618T165946
CREATED:20210107T001313Z
LAST-MODIFIED:20210107T001313Z
UID:13413-1610625600-1610625600@www.chemistry.ucla.edu
SUMMARY:Expanding the genetic code - new chemistries in living system
DESCRIPTION:Abstract: Nature uses a limited set of twenty amino acids to synthesize proteins. In recent years it has become possible to site-specifically incorporate designer amino acids with tailored chemical properties into proteins in living cells by reprogramming the genetic code. Together with developments in designing chemical reactions that are applicable to and selective within living systems\, these strategies have begun to have a direct impact on studying biological processes. \nIn this talk I will present our lab’s efforts to expand the genetic code and to endow proteins with novel chemical moieties within their physiological environment. By site-specifically incorporating artificial designer amino acids into proteins\, we have developed tools to image and probe proteins\, to study protein-protein interactions and to re-engineer and manipulate molecular networks and biological pathways in living cells. \nWe envision that these approaches and technologies will enable the study of biological processes that are difficult or impossible to address by more classical methods.
URL:https://www.chemistry.ucla.edu/seminars/expanding-genetic-code-new-chemistries-living-system/
CATEGORIES:Organic Colloquium,Seminars
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Los_Angeles:20210115T153000
DTEND;TZID=America/Los_Angeles:20210115T153000
DTSTAMP:20260618T165946
CREATED:20210104T171944Z
LAST-MODIFIED:20210104T171944Z
UID:13398-1610724600-1610724600@www.chemistry.ucla.edu
SUMMARY:Chem 268: Prof. Elizabeth Villa
DESCRIPTION:“Opening Windows into the Cell: Bringing Structure to Cell Biology Using Cryo-electron Tomography”
URL:https://www.chemistry.ucla.edu/seminars/chem-268-prof-elizabeth-villa/
CATEGORIES:Biochemistry,Seminars
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Los_Angeles:20210119T130000
DTEND;TZID=America/Los_Angeles:20210119T130000
DTSTAMP:20260618T165946
CREATED:20210113T180558Z
LAST-MODIFIED:20210113T180558Z
UID:13417-1611061200-1611061200@www.chemistry.ucla.edu
SUMMARY:NSF Center for Integrated Catalysis Webinar Series
DESCRIPTION:The NSF Center for Integrated Catalysis is delighted to announce that it will be hosting a monthly webinar series. The next webinar of this series will be held on Tuesday\, January 19th\, 2021 at 1:00 PM.  We are pleased to invite all students\, postdocs\, faculty\, and staff.
URL:https://www.chemistry.ucla.edu/seminars/nsf-center-integrated-catalysis-webinar-series-3/
CATEGORIES:Other,Seminars
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Los_Angeles:20210120T160000
DTEND;TZID=America/Los_Angeles:20210120T160000
DTSTAMP:20260618T165946
CREATED:20210106T191623Z
LAST-MODIFIED:20210106T191623Z
UID:13410-1611158400-1611158400@www.chemistry.ucla.edu
SUMMARY:Special Bio-Inorganic Chemistry Seminar
DESCRIPTION:“Chemical and Biological Design Approaches to Controlling Protons\, Electrons\, and Substrates for Sustainable Catalysis”  \nAbstract: The reductive transformation of small molecules into value-added products represents an attractive way to store sustainable energy in chemical bonds. Achieving this efficiently and selectively requires the careful management of not only the substrate and intermediates\, but also the proton and electron equivalents. Both the synthesis of small molecule catalysts and the de novodesign of metalloproteins offer the means to control these multi-component reactions. A commonly observed strategy in biological systems to lower the barrier to reductive protonation of small molecules is concerted proton-electron transfer (CPET). However\, the application of such a strategy to chemical catalysis has been lacking due to the paucity of approaches to generate CPET donors sufficiently reactive to functionalize molecules of interest ranging from N2 to ketones. Here\, I will discuss our discovery that under the protic conditions relevant to nitrogen fixation catalysis that metallocenes can serve as CPET reagents and our subsequent design of functionalized cobaltocenes suitable to electrocatalytic CPET applications. I will then finish by touching on the computational\, de novo design of non-heme iron proteins for O2-activation. These enzymes utilize a co-substrate to selectively generate a reactive metal-oxo intermediate that is useful for both C–H and olefin functionalization reactions. Nonetheless\, such enzymes have been thus far little explored in the context of protein engineering.
URL:https://www.chemistry.ucla.edu/seminars/special-bio-inorganic-chemistry-seminar-3/
CATEGORIES:Other,Seminars
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Los_Angeles:20210121T160000
DTEND;TZID=America/Los_Angeles:20210121T160000
DTSTAMP:20260618T165946
CREATED:20210107T005013Z
LAST-MODIFIED:20210107T005013Z
UID:13414-1611244800-1611244800@www.chemistry.ucla.edu
SUMMARY:Novel GABA- and Ornithine Aminotransferase Inactivators and Potential New Treatments for Epilepsy\, Addiction\, Neuropathic Pain\, and Hepatocellular Carcinoma
DESCRIPTION:Abstract: An imbalance in the levels of the inhibitory neurotransmitter g-aminobutyric acid (GABA) and the excitatory neurotransmitter L-glutamate can lead to convulsions. Inhibition of g-aminobutyric acid aminotransferase (GABA-AT)\, the enzyme responsible for the degradation of GABA\, increases brain GABA levels\, which has been shown to produce an anticonvulsant effect. Reduced brain GABA concentration also is a feature of neuropathic pain. A sharp rise in dopamine release is associated with a variety of addictive behaviors. This dopamine release can be attenuated by an increase in GABA; therefore\, inactivation of GABA-AT also has an effect on addictive behavior. Inactivation of a related enzyme\, ornithine aminotransferase (OAT) in hepatocellular carcinoma (HCC) has been shown to slow the growth of this cancer. In this lecture the design and mechanism of some of our GABA-AT inactivators will be discussed and how these compounds led to the design and discovery of CPP-115 and OV329\, potent inactivators of GABA-AT\, which have been found to have excellent pharmacokinetic and pharmacological properties for the potential treatment of epilepsy\, neuropathic pain\, and addiction. An analog related to CPP-115 was identified that does not inactivate GABA-AT but is a potent inactivator of OAT. Enzyme inactivator design and mechanism studies will be discussed\, as well as in vitro and in vivo efficacy and pharmacokinetic results\, toxicology studies\, and a clinical trial with CPP-115.
URL:https://www.chemistry.ucla.edu/seminars/novel-gaba-and-ornithine-aminotransferase-inactivators-and-potential-new-treatments/
CATEGORIES:Organic Colloquium,Seminars
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Los_Angeles:20210122T120000
DTEND;TZID=America/Los_Angeles:20210122T120000
DTSTAMP:20260618T165946
CREATED:20210114T194007Z
LAST-MODIFIED:20210114T194007Z
UID:13419-1611316800-1611316800@www.chemistry.ucla.edu
SUMMARY:Theoretical Physical Chemistry Seminar - Dr. Bingqing Cheng\, Cambridge
DESCRIPTION:Predicting material properties with the help of machine learning \nA central goal of computational physics and chemistry is to predict material properties using first-principles methods based on the fundamental laws of quantum mechanics. However\, the high computational costs of these methods typically prevent rigorous predictions of macroscopic quantities at finite temperatures\, such as chemical potential\, heat capacity and thermal conductivity. \nIn this talk\, I will first discuss how to enable such predictions by combining advanced statistical mechanics with data-driven machine learning interatomic potentials. As an example\, for the omnipresent and technologically essential system of water\, a first-principles thermodynamic description not only leads to excellent agreement with experiments\, but also reveals the crucial role of nuclear quantum fluctuations in modulating the thermodynamic stabilities of different phases of water. As another example\, we simulated the high-pressure hydrogen system with converged system size and simulation length\, and found\, contrary to established beliefs\, supercritical behaviour of liquid hydrogen above the melting line. Besides thermodynamic properties\, I will talk about how to compute the heat conductivities of liquids just from equilibrium molecular dynamics trajectories. \nDuring the second part of the talk\, I will rationalize why machine learning potentials work at all\, and in particular\, the locality argument. I’ll show that a machine learning potential trained on liquid water alone can predict the properties of diverse ice phases\, because all the local environments characterising the ice phases are found in liquid water.
URL:https://www.chemistry.ucla.edu/seminars/theoretical-physical-chemistry-seminar-dr-bingqing-cheng-cambridge/
CATEGORIES:Other,Seminars
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Los_Angeles:20210125T160000
DTEND;TZID=America/Los_Angeles:20210125T160000
DTSTAMP:20260618T165946
CREATED:20210120T182124Z
LAST-MODIFIED:20210120T182124Z
UID:13433-1611590400-1611590400@www.chemistry.ucla.edu
SUMMARY:Chem 228: Clarice D. Aiello
DESCRIPTION:
URL:https://www.chemistry.ucla.edu/seminars/chem-228-clarice-d-aiello/
CATEGORIES:Physical Chemistry Seminar,Seminars
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Los_Angeles:20210126T140000
DTEND;TZID=America/Los_Angeles:20210126T140000
DTSTAMP:20260618T165946
CREATED:20210114T233108Z
LAST-MODIFIED:20210114T233108Z
UID:13420-1611669600-1611669600@www.chemistry.ucla.edu
SUMMARY:Theoretical Physical Chemistry Seminar - Dr. Henrik Larsson\, Caltech
DESCRIPTION:Molecules in quantum motion \nIn order to fully understand the nature of chemical reactions and molecular properties\, we need to simulate both the electronic and vibrational motion quantum mechanically. However\, simulations of quantum many body systems\, such as molecules\, scale exponentially with system size. I will explain how to tame this ‘curse of dimensionality’ by combining methods from the traditionally disjoint fields of electronic structure and nuclear dynamics. This combination has enabled the simulation of complex systems with unprecedented accuracy and speed. I will demonstrate how these methods make it possible to solve a diverse set of problems\, ranging from characterizing hydrated protons on a molecular quantum level to the interaction of molecules with extreme short and intense light pulses on an attosecond time scale. I will demonstrate how these simulations provide new insight into complex experimental results.
URL:https://www.chemistry.ucla.edu/seminars/theoretical-physical-chemistry-seminar-0/
CATEGORIES:Other,Seminars
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Los_Angeles:20210127T160000
DTEND;TZID=America/Los_Angeles:20210127T160000
DTSTAMP:20260618T165946
CREATED:20210106T193712Z
LAST-MODIFIED:20210106T193712Z
UID:13411-1611763200-1611763200@www.chemistry.ucla.edu
SUMMARY:Special Bio-Inorganic Chemistry Seminar
DESCRIPTION:“ Exploring Metalloenzymes for Therapeutics and Sustainable Catalysis”  \nAbstract: Metalloenzymes are at the heart of numerous biological processes ranging from respiration and photosynthesis to natural product biosynthesis. Research in the Bhagi-Damodaran lab focuses on investigating structure\, function and reaction mechanisms of metalloenzymes\, and developing rational approaches to modulate their biological activities. Drawing from the core disciplines of biological\, inorganic\, and computational chemistry\, our group utilizes protein engineering and small molecule discovery strategies to address pressing health and energy related challenges. In this seminar\, I will describe our research efforts towards rewiring metalloenzyme-dependent redox signal transduction pathways for next-generation tuberculosis therapeutics. I will also discuss our research efforts towards re-programing non-heme iron enzymes for modular\, versatile\, and sustainable C-H bond halogenation catalysis.  
URL:https://www.chemistry.ucla.edu/seminars/special-bio-inorganic-chemistry-seminar-4/
CATEGORIES:Other,Seminars
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Los_Angeles:20210128T160000
DTEND;TZID=America/Los_Angeles:20210128T160000
DTSTAMP:20260618T165946
CREATED:20210112T010611Z
LAST-MODIFIED:20210112T010611Z
UID:13416-1611849600-1611849600@www.chemistry.ucla.edu
SUMMARY:Prioritizing the patient - The discovery of lorlatinib\, a macrocyclic ALK inhibitor for the treatment of resistant and metastatic NSCLC
DESCRIPTION:Abstract: Primary and secondary mutations in anaplastic lymphoma kinase (ALK) are oncogenic. Insights into ALK acquired resistance were used to define a drug design strategy that led to the discovery of lorlatinib (Lorbrena; PF-06463922)\, a novel ATP-competitive macrocyclic inhibitor of ALK and ROS1 kinases. Structure based drug design\, lipophilic efficiency and physicochemical property-based optimization provided inhibitors with overlapping broad-spectrum potency\, low transporter efflux\, and brain penetration. The small\, cyclic design provided a unique structure with unique properties. NMR and other analytical methods were used to study the unique molecular properties\, including atropisomerism for some analogues. Protein dynamics from x-ray crystallographic data and molecular dynamics simulations performed on ALK mutants shed light on the mechanisms of acquired resistance. Research culminated in the discovery of a first in patient candidate\, Lorbrena\, which was given Breakthrough Therapy status by the FDA in 2016 and approved in late 2018 for the treatment of patients with refractory ALK positive non-small cell lung cancer (NSCLC). Lorbrena is the first and only ALK tyrosine kinase inhibitor (TKI) approved for use after second-generation ALK TKIs. Recently\, a Phase 3 study of Lorbrena in patients with previously untreated ALK-positive\, advanced NSCLC met its primary endpoint by demonstrating significantly improved progression-free survival\, as compared to Xalkori\, which is currently primary standard of care. The FDA has accepted for Priority Review the supplemental New Drug Application (sNDA) for Lorbrena as a first-line treatment for patients with ALK-positive NSCLC based on the pivotal data from the CROWN study.
URL:https://www.chemistry.ucla.edu/seminars/prioritizing-patient-discovery-lorlatinib-macrocyclic-alk-inhibitor-treatment-resistant-and/
CATEGORIES:Organic Colloquium,Seminars
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Los_Angeles:20210129T153000
DTEND;TZID=America/Los_Angeles:20210129T153000
DTSTAMP:20260618T165946
CREATED:20210104T172053Z
LAST-MODIFIED:20210104T172053Z
UID:13399-1611934200-1611934200@www.chemistry.ucla.edu
SUMMARY:Chem 268: Prof. Tanja Kortemme
DESCRIPTION:“Switches\, sensors\, and new shapes: from design of new functions to cellular consequences of allostery”
URL:https://www.chemistry.ucla.edu/seminars/chem-268-prof-tanja-kortemme/
CATEGORIES:Biochemistry,Seminars
END:VEVENT
END:VCALENDAR