SMS Seminars

Welcome to the Fall 2021 Seminar!

Fall 2021 Seminars will be on Fridays @ 2:30pm in Biodesign Auditorium

If you have any questions regarding SMS seminars please contact:

Fall 2021 Seminars

Date Speaker Title
August 26 Hee Jeung Oh
Pennsylvania State University

Molecular Scale Engineering of Polymer Membranes
for Environment, Energy, and Health
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August 27 Jeremy Mills
Arizona State University

Computational Protein Design with Natural and Unnatural
Amino Acids
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September 3

Angel Marti
Rice University

Sensing, Studying, and Inhibiting Amyloid‐β
Aggregation using Photoluminescent Metal Complexes
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September 10 Michael D. L. Johnson 

University of Arizona

Something Old, Something New,
Something Borrowed, Copper II 
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September 17 Kimberly See


One is the Loneliest Number: Multivalent and Multielectron
Processes for Next‐Generation Batteries
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September 24 Zeliha Kilic
St. Jude’s
Data‐driven approaches for modeling and analysis in
Biophysics and Biochemistry
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October 1 Elisa Franco
University of California, Los Angeles

Dynamic Self‐assembly of Encapsulated DNA Nanotubes
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October 8 Jonathan Schlebach

Indiana University Bloomington

Impact of Co‐ and Post‐Translational Folding Constraints on
the Mutational Tolerance of Integral Membrane Proteins
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October 15 Lisa Jones
University of Maryland

In‐Cell Protein Footprinting Coupled with Mass
Spectrometry for Structural Biology Across the Proteome
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October 15 Gavin Knott
Monash University, Australia
Mechanisms and Applications of CRISPR‐Cas RNA Sensors
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October 22

Josh Vermaas

Michigan State University

Exploring Biological Mechanisms and Materials
Through Molecular Simulation for a Sustainable Bioeconomy
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November 4 Eyring Lecture: Mario Capecchi

University of Utah

The Making of a Scientist: An Unlikely Journey

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November 5 Eyring Lecture: Mario Capecchi

University of Utah

Mutant Hoxb8 Microglia Are Causative for Chronic Anxiety
and OCD‐Spectrum Disorders in Mice
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November 12 Dor Ben-Amotz

Purdue University

Surfactant Aggregate Size Distributions Above and
Below the Critical Micelle Concentration
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November 19 O'Keeffe Inaugural: Omar Yaghi

University of California Berkeley

Reticular Chemistry and Materials
for Water Harvesting from Air Anytime Anywhere
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Eyring Seminar

About: Eyring Lectures in Chemistry and Biochemistry

The Eyring Lectures in Chemistry and Biochemistry is an interdisciplinary distinguished lecturer series dedicated to stimulating discussions by renowned scientists who are at the cutting edge of their respective fields. Each lecture series consists of a lead-off presentation to help communicate the excitement and challenge of this central science to the University and community, followed by a more specialized colloquium to help bring the audience to the scientific frontiers of the topics under discussion. Speakers will be scholars in residence in the Department during their lecture series and will be available for informal discussions with faculty, students, and other interested individuals.

The Eyring Lectures in Chemistry and Biochemistry bears the name of our colleague LeRoy Eyring, Regents' Professor of Chemistry, whose extraordinary instructional and research accomplishments and professional leadership at Arizona State University helped to bring the School of Molecular Sciences into international prominence.

Eyring Lecturer Fall 2021

Mario Capecchi
University of Utah

  • General Lecture
    The Making of a Scientist: An Unlikely Journey
    Thursday Nov 4
    6:00 PM, Biodesign Auditorium
  • Technical Presentation
    Mutant Hoxb8 Microglia Are Causative for Chronic Anxiety and OCD‐Spectrum Disorders in Mice. 
    Friday Nov 5
    2:30pm, Biodesign Auditorium

Download PDF- Nov 4th Lecture  || Download PDF- Nov 5th Lecture

Eyring Lecturer Fall & Spring 2019

Steven Boxer
Camille Dreyfus Professor of Chemistry
Stanford University

  • General Lecture
    GFP - the Green Revolution Continues
    Thursday, 11/14/2019
    6:30 PM, PSH-153

Bioluminescence has fascinated scientists since ancient times – the green fluorescence from agitated jellyfish is an example and this comes from Green Fluorescent Protein (GFP). Since the discovery in the mid-1990’s that GFP can be expressed in essentially any organism, GFPs have become indispensable tools as genetically encoded fluorescent reporters. A bewildering array of variants has been developed leading to a wide pallet of colors and photo-switching characteristics that are essential for super-resolution microscopy. Our lab was involved in early studies of excited state properties of GFP that led to the discovery that the GFP chromophore is a photoacid – this has many consequences for further protein design and is related to the natural function of this unusual protein. Beyond applications in imaging, GFPs are a wonderful model system for probing the spectroscopic and functional consequences of the interaction between a prosthetic group and the protein surrounding it. I will discuss several examples related to photoisomerization of the chromophore. (1) We have systematically altered the electrostatic properties of the GFP chromophore in a photo-switchable variant using amber suppression to introduce electron-donating and -withdrawing groups to the phenolate ring. The contributions of sterics and electrostatics can be evaluated quantitatively and used to demonstrate how electrostatic effects bias the pathway of chromophore isomerization. (2) Split GFPs are made from protein fragments whose reassembly leads to a fluorescent readout. By chance, we discovered that split -strands can be photo- dissociated, i.e. split GFP is a genetically encoded caged protein. The mechanism of this unusual process will be discussed along with possible applications as optogenetic tools. Host: Neal Woodbury

  • Technical Presentation
    Electric Fields and Enzyme Catalysis
    Fridays, 11/15/2019
    1:30 PM, in Biodesign B (BDB) Auditorium B105

We have developed the vibrational Stark effect to probe electrostatics and dynamics in organized systems, in particular in proteins where vibrational probes can report on functionally important electric fields. The strategy involves deploying site-specific vibrational probes whose sensitivity to an electric field is measured in a calibrated external electric field. Once calibrated, these probes, typically nitriles or carbonyls, can be used to probe changes in electric field due to mutations, ligand binding, pH effects, light-induced structural changes, etc. We can also obtain information on absolute fields by combining vibrational solvatochromism and MD simulations, checked by the vibrational Stark effect calibration. This frequency-field calibration can be applied to quantify functionally relevant electric fields at the active site of enzymes. Using ketosteroid isomerase as a model system, we correlate the field sensed at the bond involved in enzymatic catalysis with the rate of the reaction it catalyzes, including variations in this rate in a series of mutants and variants using non-canonical amino acids. This provides the first direct connection between electric fields and function: for this system electrostatic interactions are a dominant contribution to catalytic proficiency. Using the vibrational Stark effect, we can now consistently re-interpret results already in the literature and provide a framework for parsing the electrostatic contribution to catalysis in both biological and non-biological systems. Extensions of this approach to other classes of enzymes, to effects of electrostatics on pathways of photoisomerization in proteins, and to the evolutionary trajectories of enzymes responsible for antibiotic resistance will be described if time permits. Host: Neal Woodbury

Dean Emily Carter
Princeton University

  • General Lecture
    "Sustainable Energy Materials from First Principles "
    Thursday, March 21, 2019
    6:30 PM, PSH-153

I believe that we scientists and engineers have a responsibility to use our skills to improve life for all Earth’s inhabitants. To this end, for the past dozen years, I have used my skills - in developing and applying quantum mechanics simulation methods aimed at complex phenomena difficult to probe experimentally - to help accelerate discovery, understanding, and optimization of materials for sustainable energy conversion processes. These range from materials for converting sunlight and other renewable energy sources to fuels and electricity, to biodiesel fuels, to clean electricity production from solid oxide fuel cells and nuclear fusion reactors, to lightweight metal alloys for fuel-efficient vehicles. During this talk, I will focus on potential technological advances in materials science, nanoscale optics, and electrochemistry that could someday create a virtuous cycle, exploiting energy from sunlight and molecules in air, water, and carbon dioxide to synthesize the fuels and chemicals needed to sustain future generations.

Eyring Lecturer Fall & Spring 2018

Sunney Xie
Department of Chemistry and Chemical Biology
Harvard University & Peking University

  • Technical Presentation
    "Stimulated Raman Scattering Microscopy: Seeing the Invisible in Biology and Medicine"

    Wednesday, 10/24/2018
    3:30 PM
    Biodesign Auditorium BDB105

Stimulated Raman scattering (SRS) microscopy is a label-free and noninvasive imaging technique using vibration spectroscopy as the contrast mechanism. Recent advances have allowed significant improvements in sensitivity, selectivity, robustness, and cost reduction, opening a wide range of applications. This is particularly relevant in biology since SRS microscopy does not affect cell function, and is best suited for imaging small metabolite molecules. For medicine, SRS microscopy provides instant tissue examination without the need of previous histological staining procedures. Host: Neal Woodbury and Jia Guo

  • General Lecture
    "Life at the Single Molecule Level: From Single Molecule Enzymology to Single Cell Genomics"

    Thursday, 10/25/2018
    6:30 PM, PSH-153

Since the 1990s, developments in room-temperature single-molecule spectroscopy, imaging, and manipulation have allowed studies of single-molecule behaviors in vitro and in living cells. Unlike conventional ensemble studies, single-molecule enzymology is characterized by ubiquitous fluctuations of molecular properties. The understanding of such single-molecule stochasticity is pertinent to many life processes. DNA exists as single molecules in an individual cell. Consequently, gene expression is stochastic. Single-molecule gene expression experiments in live single cells have allowed quantitative description and mechanistic interpretations. The fact that there are 46 different individual DNA molecules (chromosomes) in a human cell dictates that genomic variations, such as copy-number variations (CNVs) and single nucleotide variations (SNVs), occur stochastically and cannot be synchronized among individual cells. Probing such genomic variations requires single-cell and single-molecule measurements, which have only recently become possible. These studies are difficult since they require the amplification of the minute amount of DNA of a single cell, and existing single-cell whole genome amplification (WGA) methods have been limited by low accuracy of CNV and SNV detection. We have developed transposase-based methods for single-cell WGA, which have superseded previous methods. With the improved genome coverage of our new WGA method, we developed a high-resolution single-cell chromatin conformation capture method, which allows for the first 3D genome map of a human diploid cell. We have also developed a method for single-cell transcriptome with better detection efficiency and accuracy, revealing intrinsic correlations among all detected mRNAs in a single-cell. Host: Neal Woodbury and Jia Guo

David Baker
Professor of Biochemistry
Head of the Institute for Protein Design
Department of Chemistry
University of Washington

  • General Lecture
    "The Coming of Age of De Novo Protein Design"

    Thursday, 3/29/2018
    6:30 PM, PSH-150

The advances in de novo protein design described in my first talk are opening up many new exciting areas of application. I will describe our efforts towards designing next generation therapeutics, vaccines and functional nanomaterials with applications ranging from computing to light harvesting. Host: Neal Woodbury and Jeremy Mills

  • Technical Presentation
    "Recent Advances in Olefin Metathesis by Molybdenum and Tungsten Catalysts"

    3:40 PM, PSH-151

Proteins mediate the critical processes of life and beautifully solve the challenges faced during the evolution of modern organisms. Our goal is to design a new generation of proteins that address current day problems not faced during evolution. In contrast to traditional protein engineering efforts, which have focused on modifying naturally occurring proteins, we design new proteins from scratch based on Anfinsen’s principle that proteins fold to their global free energy minimum. We compute amino acid sequences predicted to fold into proteins with new structures and functions, produce synthetic genes encoding these sequences, and characterize them experimentally. I will describe the design of ultra-stable idealized proteins, flu neutralizing proteins, high affinity ligand binding proteins, and self-assembling protein nanomaterials. I will also describe the contributions of the general public to these efforts through the distributed computing project Rosetta@Home and the online protein folding and design game Foldit. Host: Neal Woodboury and Jeremy Mills

Eyring Lecturer Fall & Spring 2017

Richard Royce Schrock
F G Keyes Professor of Chemistry
MIT Chemistry

  • General Lecture
    "A Discovery and a Nobel Prize 30 years Later";

    Thursday, 10/19/2017
    6:30 PM, PSH-150

A catalytic reaction discovered in the 1960s allows one to break carbon-carbon double bonds and form new ones with remarkable ease. This "metathesis" reaction began to attract the interest of organic, inorganic, and polymer chemists because of its great potential in manipulating carbon-carbon bonds, which is a fundamental goal of organic chemistry. The metathesis reaction has continued to change how chemistry that involves carbon-carbon double bonds, in particular, is practiced in the laboratory and industry. In 1974 I was in the right place at the right time to make a discovery that helped us understand how this reaction works and have spent my career developing catalysts for it. In the process I also discovered catalysts that "metathesize" carbon-carbon triple bonds and one that will "break" the triple bond in dinitrogen (to give ammonia catalytically), a reaction that is crucial to all life on earth. Host: Neal Woodbury

  • Technical Presentation
    "Recent Advances in Olefin Metathesis by Molybdenum and Tungsten Catalysts"

    3:40 PM, PSH-151

Advances in applications of the chemistry of Mo and W olefin metathesis catalysts in the last two years include the synthesis of monoaryloxide chloride imido catalysts, kinetically Z- or E-selective catalytic macrocyclic ring-closing metathesis, stereoselective (Z or E) olefin metathesis reactions that use electron-poor olefins (ClCH=CHCl and CF3CH=CHCF3), and ROMP reactions that yield cis,syndiotactic-A-alt-B copolymers from enantiomerically pure monomers. New applications rely on synthetic advances that include new approaches to monoaryloxide chloride complexes, to rare molybdenum oxo alkylidene complexes, and to previously unknown Mo=CHCl and Mo=CHCF3 complexes, which must be involved in reactions with the electron-poor olefins ClCH=CHCl and CF3CH=CHCF3. Host: Neal Woodbury

Gerhard Wagner
Professor, Department of Biological Chemistry and Molecular Pharmacology
Harvard Medical School

  • General Lecture
    "Solution NMR: from a Chemist's Tool to Solving Protein";

    Thursday, 4/13/2017
    6:30 PM, PSH-150

When I became interested in biophysics little had been done in protein NMR. Mainly chemists used NMR to check the success and purity of their reaction products. As undergraduate physics student at the Technical University of Munich, I had worked on Mössbauer effect studies hemoglobins and ferredoxins. While this technology yields spectra with a small number of resonance lines, I learned that NMR spectroscopy of the same class of proteins could yield spectra with numerous resonances as was shown at Bell Labs in the Shulman group. The discoverer of the paramagnetically shifted heme resonances, Kurt Wüthrich had just moved to the ETH in Zürich, and I decided to join his group as a graduate student. Thus, I entered the field of protein NMR at an early stage. First, I focused on internal motions of proteins and discovered that aromatic side chains of the basic pancreatic trypsin inhibitor (BPTI) rotate fast or slowly depending on their location, and NMR could measure rotation rates. Fast ring flipping was unexpected since aromatic side chains appeared rigidly oriented in the high-resolution crystal structures becoming available at that time. With new NMR instruments available I developed procedures for sequentially assigning the entire 1H NMR spectrum of BPTI, the first NMR assignment of a protein, and it appeared possible that with a skillful use of the nuclear Overhauser effect (NOE) it should be possible to determine protein structures with NMR. However, the first structure of BPTI I determined together with Werner Braun was of very low resolution due to the lack of better reconstruction software and was never published. When more powerful software packages were developed by Werner Braun and Tim Havel, I determined the structure of the protein metallothionein-2, which appeared entirely different from a X-ray structure of the same protein just published in Science; however, after much checking our NMR structure was found to be correct. After my time at the ETH I moved to the University of Michigan where we developed the first 1H-15N-13C triple resonance experiments and also started to measure 13C and 15N relaxation rates to characterize backbone dynamics of proteins. In 1990 I moved to Harvard Medical School and became very interested in tackling biological problems including proteins related to T-cell activation. Soon I became interested in translation initiation, and my group determined structures of several proteins that play key roles in protein synthesis. Subsequently, we discovered small molecule inhibitors of translation initiation that have anti-tumor activity, and we still pursue this research activity. More recently, my group focused on membrane proteins and we developed new procedures for covalently circularizing membrane scaffolding proteins to create well-defined membrane surrogates for structural and functional studies of membrane proteins. Host: Neal Woodbury

  • Technical Presentation
    "Engineering Phospholipid Nanodiscs for Membrane Protein Studies"

    3:40 PM, PSH-151

Biophysical studies of membrane proteins face multiple obstacles, including low expression yield, sample heterogeneity and the need for a membrane mimetic that resemble the native environment. When using NMR spectroscopy, additional problems are the large size of the systems and the need of incorporating stable isotope 13C, 15N and 2H. Micelles, or bicelles, which are frequently used for structural studies of membrane proteins, but have the disadvantage of the destabilizing effect of the detergents, in particular when the membrane proteins have water-soluble domains or interact with soluble proteins. Therefore, we embraced the use of phospholipid nanodiscs for membrane protein studies. Nanodiscs are patches of phospholipid bilayer surrounded by two copies of a membrane-scaffolding protein (Msp1), which is derived from apolipoprotein A1. We had shown that the Voltage-Dependent Anion Channel (VDAC1) can be inserted into nanodiscs and can be analyzed both in EM images and in NMR spectra. However, embedding was heterogeneous and prevented detailed NMR analysis. To address this problem and adapt nanodiscs to different size membrane proteins we first engineered Msp1 variants that yield nanodiscs at diameters of 9.5, 8.1, 7.8 and 6.8 nm, and we could determine an NMR structure of OmpX in the 8.1 nm nanodisc. However, the diameter distribution of these nanodiscs is rather wide. To further optimize nanodiscs, we developed procedures to covalently circularize the scaffolding protein and make nanodiscs of exactly defined diameters. We could extend the cND sizes from as low as 8 nm to as high as 50 nm each exhibiting a very narrow size distribution. We are able to insert membrane protein into the covalently circularized nanodiscs, record NMR spectra for smaller systems and obtain negative stain or cryo EM images from nanodisc-bound membrane proteins. We pursued applications from small mitochondrial membrane proteins to GPCRs and larger systems. Host: Neal Woodbury

Eyring Lecturer Fall & Spring 2016

Nobel Laureate Thomas R. Cech
Distinguished Professor, University of Colorado Boulder
Director, University of Colorado BioFrontiers Institute

- Nobel Prize in Chemistry 1989, National Medal of Science 1995

  • General Lecture
    "The Long Road to Precision Medicine: How Mutations Activate an “Immortality Gene” and Help Drive Cancer"

    Thursday, 11/03/2016
    6:30 PM, PSH-150

The practice of medicine has continually evolved towards greater precision. Now in the last decade, the availability of genomic and other –omic information has provided the opportunity for a quantum leap in precision. Yet the road towards precision medicine is long, and many obstacles interfere. Dr. Cech will give an example involving his own work on telomerase, which may perhaps contribute to more precise cancer treatment in the future. Host: Neal Woodbury and Julian Chen

  • Technical Presentation
    "LncRNAs, Histone Modification, and Epigenetic Silencing in Cancer"

    Friday, 11/04/2016
    3:40 PM, PSH-151

Polycomb repressive complex 2 (PRC2) is a multi-subunit complex, catalyzing trimethylation of H3K27 of nucleosomes. Such methylation marks promote epigenetic silencing of chromatin during embryonic development and cancer. Long noncoding (lnc) RNAs have been suggested to recruit PRC2 to its sites of action on chromatin. By studying the binding of PRC2 to RNA in vitro and in vivo, we and others have found that it binds RNA promiscuously – almost any RNA will bind. Yet we also find some special RNAs that have huge differences in affinity. How can we reconcile these observations, and what might they mean for epigenetic silencing? Host: Neal Woodbury and Julian Chen

Eyring Lecturer Fall & Spring 2015

Cynthia J. Burrows
Distinguished Professor, Thatcher Presidential Endowed Chair of Biological Chemistry
Department of Chemistry, The University of Utah

  • General Lecture
    "Peering into the Dark Matter of DNA: Structures and Functions beyond Watson & Crick"

    Thursday, 11/5/2015
    6:30 PM, PSH-151

Less than 2% of the human genome codes for the amino acid sequence of proteins. Why is all the rest of the DNA there? Some of it participates in orchestrating replication, some in the protection of the ends (telomeres), and some sections upstream of transcription start sites (promoters) control whether or not a gene is expressed as protein. All of these functions of DNA include guanine-rich sequences capable of folding into G-quadruplexes, four-stranded folds of DNA that differ dramatically from the classical base-pairing scheme of the Watson-Crick double helix. Furthermore, the G-rich sequences are sensitive to oxidative stress, converting to modified structures including 8-oxo-7,8-dihydroguanine (OG) and the hyperoxidized lesions spiroiminodihydantoin (Sp) and guanidinohydantoin (Gh). Both the overall reactivity of a G residue in DNA or RNA and the final oxidized G product formed are highly dependent on sequence, solvent exposure and mechanism. For example, oxidation of G in G-quadruplex folds leads to very different outcomes compared to those in Watson-Crick B-helical duplexes. The location of G damage in turn has a profound effect on the stability of duplex vs. quadruplex structures. We propose that G-rich sequences respond to oxidative stress by selecting a secondary structure that can best accommodate the damaged base, and that ‘shape-shifting’ may be used as a signaling mechanism to affect transcription and repair. The implications are that nucleotide identity beyond the exome may be important in gene expression and disease, and that the definition of epigenetic modifications should be expanded to include guanine oxidation. Host: Dan Buttry

  • Technical Presentation
    “Single-Molecule Analysis of the Effects of Oxidative Stress on G:C-rich Sequences in DNA”

    Friday, 11/6/2015
    3:40 PM, PSH-151

Oxidative stress in the cell results in modifications to DNA and RNA bases and downstream events including effects on transcription and replication as well as signaling for repair. Ultimately, unrepaired damage in DNA leads to mutagenesis that is a contributing factor to cancer and other diseases. Our studies focus on base modifications arising from guanine (G) oxidation, including how and where they form in the genome. To investigate this, we have developed a single-molecule nanopore approach that is complementary to other biophysical techniques for interrogating nucleic acid structure. Specifically, the electrophoretic capture of DNA strands, either Watson-Crick duplexes or folded G-quadruplexes, inside a protein nanopore (alpha-hemolysin) embedded in a lipid bilayer provides information about the presence of oxidized bases as well as the dynamics of unfolding. In order to adapt this methodology to sequencing DNA for modified bases, we have developed a protocol for PCR amplification using a third base pair to mark the site of DNA modification. Host: Dan Buttry

Tobin J. Marks
Vladimir N. Ipatieff Professor of Chemistry and Professor of Materials Science and Engineering
Department of Chemistry, Materials Research Center, and the Argonne-Northwestern Solar Research Center, Northwestern University

  • General Lecture
    " Interface Science of Plastic Solar Cells"

    Thursday, 2/12/2015
    6:30 PM, PSH-150

Interface Science of Organic Photovoltaics Tobin J. Marks Department of Chemistry, Materials Research Center, and the Argonne-Northwestern Solar Research Center Northwestern University, Evanston IL 60208, USA The ability to fabricate molecularly tailored interfaces with nanoscale precision offers means to selectively modulate charge transport, molecular assembly, and exciton dynamics at hard matter-soft matter and soft-soft matter interfaces. Such interfaces can facilitate transport of the “correct charges” while blocking transport of the “incorrect charges” at the electrode-active layer interfaces of organic photovoltaic cells. This interfacial tailoring can also suppress carrier-trapping defect densities at interfaces and stabilize them with respect to physical/thermal de-cohesion. For soft matter-soft matter interfaces, interfacial tailoring can also facilitate exciton scission and photocurrent generation in such cells. In this lecture, challenges and opportunities in organic photovoltaic interface science are illustrated for four specific and interrelated areas of research: 1) controlling charge transport across hard matter(electrode)-soft matter interfaces in organic photovoltaic cells, 2) controlling charge transport by specific active layer nano/microstructural organization in the bulk active material and at the electrodes, 3) controlling exciton dynamics and carrier generation at donor-acceptor interfaces in the active layer, 4) designing transparent conducting electrodes with improved properties. It will be seen that such rational interface engineering along with improved bulk-heterojunction polymer structures guided by theoretical/computational analysis affords exceptional fill factors, solar power conversion efficiencies greater than 9%, and enhanced cell durability. Host: Dan Buttry

  • Technical Presentation
    "Thermochemically Leveraged Strategies for Biofeedstock Catalysis"

    Friday, 2/13/2015
    3:40 PM, PSH-151

Thermodynamic Strategies for New Catalytic Process Design. Biofeedstock Processing via Tandem C-O Hydrogenolysis Tobin J. Marks Northwestern University, Evanston IL 60208 USA Abstract This lecture focuses on thermodynamics/mechanism-based strategies for converting abundant biofeedstocks into useful chemicals. Thus, new approaches to the hydrogenolysis of C-O bonds are discussed with the ultimate goal being the processing of diverse biomass feedstocks. It is shown that selective hydrogenolysis of cyclic and linear etheric C-O bonds is effected by a tandem catalytic system consisting of recyclable metal triflate Lewis acids and supported palladium nanoparticles or related catalysts in either “green” ionic liquid solvents or in the neat substrates. In this tandem process, the metal homogeneous triflates catalyze the endothermic retro-hydroalkoxylation of the ether, with the supported palladium catalyst subsequently catalyzing the hydrogenation of the resulting intermediate alkenols, to afford saturated alkanols with high overall activity and selectivity. Kinetic and DFT computational studies show that the turnover-limiting step in these reactions is the retro-hydroalkoxylation, followed by rapid alkenol hydrogenation. Furthermore, the metal triflate catalytic activity scales approximately with the DFT-computed charge density on the triflate metal ion. With the most active of these catalysts, ethereal substrates are rapidly converted, via the alkenol, to the corresponding saturated hydrocarbons. In similar tandem processes, it is shown that esters and triglycerides are also rapidly and selectively converted to alcohols and, ultimately, to saturated hydrocarbons. The kinetics and mechanism of these ester hydrogenolysis processes, as deduced by experimental results and DFT computation, are compared and contrasted with those of the corresponding ethers Host: Dan Buttry

Eyring Lecturer Fall & Spring 2014

Peter G. Schultz
Professor of Chemistry, The Scripps Research Institute, La Jolla, CA

  • General Lecture
    "An Expanding Genetic Code"

    Thursday, 11/13/2014
    6:30 PM, PSH-152

  • Technical Presentation
    "A Chemist's Foray into Translational Research"

    Friday, 11/14/2014
    3:40 PM, PSH-151

Richard P. Van Duyne
Charles E. and Emma H. Morrison Professor of Chemistry, Professor of Biomedical Engineering, and Professor in the Applied Physics program at Northwestern University

  • General Lecture
    “Molecular Plasmonics: Nanoscale Spectroscopy and Sensing"

    Thursday, 2/20/2014
    7:30 PM, PSH-151

  • Technical Presentation
    “New Tools for the Study of Single Molecule Chemistry at the Atomic Length Scale and Femtosecond Time Scale”

    Friday, 2/21/2014
    3:40 PM, PSH-151

Eyring Lecturer Fall & Spring 2013

Carolyn Bertozzi
Department of Chemistry, Department of Molecular and Cell Biology, University of California Berkeley

    Illuminating Sugars: The "dark matter" of the cell surface

    Thursday, October 31, 2013
    7:30 p.m., PSH-151

    Bioorthogonal Chemistry: An enabling tool for biology and drug development

    Friday, November 1, 2013
    3:40 p.m., PSH-151

Geri Richmond
Richard M. and Patricia H. Noyes Professor,
Department of Chemistry , University of Oregon

    At the Water’s Edge:

    Understanding Environmentally Important Processes at Aqueous Surfaces
    Thursday, February 7, 2013
    7:30 p.m., PSH-152

    Line ‘Em All Up:

    Macromolecular and Nanoparticle Assembly at Liquid Surfaces
    Friday, February 8, 2013
    11:30 a.m., PSH-152

Eyring Lecturer Fall & Spring 2012

Carl Lineberger
E. U. Condon Distinguished Professor of Chemistry and Biochemistry
University of Colorado, Boulder

    Anion Chemistry Research, and How it Led to “A Look Inside the World of Science and Technology Policy”.

    Thursday, 11/8/2012 7:30 PM, PS H151

    Molecular Reaction Dynamics in Time and Frequency Domains: A Wonderful Playground for Collaboration between Experiment and Theory

    Friday, 11/9/2012 3:40 PM, PS H151

Kendall N. Houk
Department of Chemistry & Biochemistry

    "Designing New Enzymes"

    Thursday, January 26 7:30 p.m., PS H-150

    "Dynamics, Mechanisms and Applications of Cycloadditions"

    Friday, January 27 3:30 p.m., PS H-151