Friday, April 20, 1:30pm - 2:30pm, NHB 1.720
Professor of Chemistry
Penn State University
The laboratory of Biointerfaces, led by Prof. Paul Cremer, is a multidisciplinary research team that works at the crossroads of biological interfaces, manomaterials, spectroscopy, and microfluidics. Biophysical and analytical studies are tied together through the employment of novel lab-on-a-chip platforms which enable high throughput/low sample volume analysis to be performed with unprecedented signal-to-noise. From neurodegenerative diseases to artificial hip implants, a huge variety of processes occur at biological interfaces. Our laboratory uses a wide variety of surface specific spectroscopies and microfluidic technologies to probe mechanisms of disease, build new biosensors against pathogens, and understand the molecular-level details of the water layer hugging a cell membrane.
h-index: 59 Total Publications: 134 Total Citations: 12,064 (Web of Science, Mar. 2018)
Thursday, April 5, 3:30pm - 4:30pm, WEL 2.122
Assistant Professor of Chemistry
The central theme of the Ardo Group's research program is to understand and control reaction mechanisms at interfaces, with the goal of optimizing energy conversion for practical applications, including solar seawater desalination, solar fuels devices, photovoltaics, redox flow batteries, and fuel cells.
h-index: 20 Total Publications: 38 Total Citations: 2255 (Web of Science, Mar. 2018)
Thursday, March 29, 3:30pm - 5:00pm, WEL 2.122
Assistant Professor of Chemistry
Ohio State University
Recent innovation in mass spectrometry (MS) is the ability to generate intact molecular ions, focus and use them as ordinary reagents for organic reactions at ambient surface, outside the mass spectrometer. Most projects in the Badu lab build on this innovation, but instead of simple organic compounds, we focus on drugs and biomolecules of specific biological importance.
h-index: 14 Total Publications: 25 Total Citations: 482 (Web of Science, Mar. 2018)
h-index: 14 Total Publications: 26 Total Citations: 538 (Scopus, Mar. 2018)
George and Pauline Watt Centennial Lectureship
Monday, March 26, 2018, 03:30pm - 04:30pm, WEL 2.122
Distinguished Professor, Chemistry
Physical/chemical: fluorescence correlation spectroscopy (FCS); high resolution cryo-electron microscopy (cryo-EM); magnetic and optical tweezers (Professors James Bowie (UCLA) and Doug Smith (UCSD)) maleimide and “click” chemistries for conjugating ligands to capsid protein; electrophoretic, sedimentation, and chromatographic separations and analyses of fluorescently-labeled RNA, protein, and RNA-protein complexes; labeling of RNA ends, and of capsid proteins, by <2nm gold particles; statistical-mechanical modeling.
Biological: agrobacterial transformation of plants for high-level expression of wildtype and mutant CCMV capsid protein; genetic engineering of RNA-virus-derived replicons from mammalian, insect, and plant viruses; transfection and infection of cultured cells for assays of RNA replication and protein expression levels; in vitro transcription and genetic engineering of viral genes and their protein products; cell-free translation of RNA, of virus-like particles, and of viruses.
h-index: 69 Total Publications: 221 Total Citations: 20,814 (Web of Science, Mar. 2018)
h-index: 58 Total Publications: 178 Total Citations: 10,742 (Scopus, Mar. 2018)
Friday, March 23, 3:30pm - 5:00pm, WEL 2.122
Faculty, Dept. of Chemistry
University of Rome La Sapienza
h-index: 25 Total Publications: 107 Total Citations: 1790 (Web of Science, Feb. 2018)
h-index: 26 Total Publications: 112 Total Citations: 1785 (Scopus, Feb. 2018)
h-index: 28 Total Citations: 2083 (Google Scholar Citations, Feb. 2018)
TO BE RESCHEDULED
Elizabeth Pierson currently works at the Research Laboratories, Merck. Elizabeth does research in Analytical Chemistry, Virology and Molecular Biology. Their current project is 'Analytical Research and Development of Formulated Small Molecule and Biological Pharmaceuticals.'
W. Albert Noyes, Jr. Distinguished Visiting Lectureship
Thursday, March 1, 3:30pm - 4:30pm, WEL 2.122
Professor of Biochemistry, Biophysics and Structural Biology
The long-term goal of our research is to understand the structural and dynamic information encoded in the linear sequence of amino acids. Proteins undergo an incredible transformation from one-dimensional sequence information into complex three-dimensional shapes that carry out intricate cellular functions. We still, however, don't have enough biophysical knowledge to translate this sequence information into functional insights. For instance, many proteins share the same native structure yet their cellular dynamics and function, in other words their energy landscapes, are different. Our laboratory uses a combination of biophysical, structural and computational techniques to understand these features.
h-index: 42 Total Publications: 97 Total Citations: 7040 (Web of Science, Feb. 2018)
h-index: 42 Total Publications: 110 Total Citations: 7048 (Scopus, Feb. 2018)
Thursday, February 22, 3:30pm - 4:30pm, WEL 2.122
Research in the Dyer group spans a broad range of problems in biophysical and bioinorganic chemistry. Links to the three main focus areas are included below: mapping protein folding energy landscapes, exploring the role of protein dynamics in enzymatic catalysis, and developing photocatalysts for solar water splitting and hydrogen production. We have also undertaken a collaboration with the Salaita lab, funded by DARPA, to exploit coupled enzymatic reactions for induced mechanical work.
Two unifying themes of this work are exploring the role of dynamics in protein structure and function and the development and application of new laser and spectroscopic tools for the study of protein dynamics. Our work effectively cuts across traditional disciplines with an emphasis on using quantitative physical methods to address biological problems. For example, our study of fast events in protein folding integrates efforts in mechanical engineering (microfluidics for ultrafast mixing), physical chemistry (spectroscopy, fast kinetics, physical models), molecular biology (mutants, protein folding models) and theoretical chemistry (MD simulations of folding). We emphasize the use of spectroscopic techniques with high structural specificity and time resolution, such as isotope edited infrared spectroscopy to elucidate the functional dynamics of proteins on all relevant timescales.
h-index: 50 Total Citations: 6897 (Google Scholar, Feb. 2018)
h-index: 45 Total Publications: 131 Total Citations: 5637 (Web of Science, Feb. 2018)
Wednesday, February 21, 3:30pm - 4:30pm, WEL 2.122
Our research focuses on developing and applying state-of-the-art single-molecule methods to characterize and understand the properties of nanoscale materials and biological systems. Compared with traditional ensemble measurements, the single molecule approach removes ensemble averaging, so that distributions and fluctuations of molecular properties can be characterized and transient intermediates identified. The single-molecule techniques we employ include single-molecule fluorescence imaging, single-molecule FRET, single-molecule tracking, super-resolution localization microscopy, and magnetic tweezers. Our research program provides students with scientific training spanning from sophisticated microscopy/spectroscopy techniques, rigorous data analyses to protein and genetic engineering using modern molecular biology techniques, as well as nanotechnology and nanomaterials.
h-index: 31 Total Publications: 57 Total Citations: 4069 (Google Scholar, Feb. 2018)
Thursday, February 15, 3:30pm - 5:00pm, WEL 2.122
The Mirkin Research Group focuses on developing methods for controlling the architecture of molecules and materials on the 1 – 100 nm length scale, understanding their fundamental properties, and utilizing such structures to develop novel tools that can be applied in the areas of chemical and biological sensing, gene regulation, immunomodulation, lithography, catalysis, optics, and energy generation, storage, and conversion.
The Mirkin Research Group has pioneered the use of nanoparticle-biomolecule conjugates as synthons in materials science and the development of many nanoparticle-based extra- and intracellular biodiagnostic and therapeutic tools.
h-index: 132 Total Publications: 607 Total Citations: 87,238 (Web of Science, Jan. 2018)
Highly Cited: 46 Articles
h-index: 135 Total Publications: 705 Total Citations: 90,931 (Scopus, Feb. 2018)
Thursday, February 8, 3:30pm - 4:30pm, WEL 2.122
Professor, Chemical Physiology
Scripps Research Institute
Research in the Yates lab is focused on the development and application of mass spectrometry-based proteomics techniques to a wide range of biological questions. Our lab has been instrumental in the evolution of the field to its current status, having pioneered many of the landmark advances that form the basis for prevailing proteomics practices, including shotgun proteomics (McCormack, A. L.; Schieltz, D. M.; Goode, B.; Yang, S.; Barnes, G.; Drubin, D.; Yates, J. R., III. Anal. Chem. 1997, 69, 767−776), database searching (SEQUEST, Eng, J. K.; McCormack, A. L.; Yates, J. R., III. J. Am. Soc. Mass Spectrom. 1994, 5, 976−989), and Multidimensional Protein Identification Technology (MudPIT, Washburn, M. P.; Wolters, D.; Yates, J. R., III. Nat. Biotechnol. 2001, 19, 242−247). We continue the drive to increase the scope, sensitivity and throughput of proteomics technologies and their application to biological questions.
Our research encompasses the areas of bioinformatics and software development, methods development and biological applications. The integration of all the elements in the proteomics pipeline within one lab facilitates advances in all of them.
The Yates lab has published more than 700 peer reviewed papers. Recent highlights include comprehensive proteomics studies revealing molecular mechanisms implicated in Cystic Fibrosis as well as identification of proteins capable of restoring function to mutated proteins in the disease, and investigations into affective disorders of the brain, including schizophrenia and depression.
h-index: 132 Total Publications: 708 Total Citations: 69,178 (Web of Science, Jan. 2018)
Thursday, February 1, 3:30pm - 5:00pm, WEL 2.122
Assistant Professor, Chemistry
h-index: 12 Total Publications: 27 Total Citations: 975 (Web of Science, Jan. 2018)
Thursday, January 25, 3:30pm - 4:30pm, WEL 2.122
Associate Professor, Chemistry
University of Louisville
h-index: 35 Total Publications: 81 Total Citations: 3313 (Web of Science, Dec. 2017)
Highly Cited Paper: Mieszawska, AJ et al. The synthesis and fabrication of one-dimensional nanoscale heterojunctions. Small, 3(5), 2007, 722-756. DOI: 10.1002/smll.200600727
Faculty Recruiting Seminar
Thursday, January 18, 3:30pm - 5:00pm, WEL 2.122
Postdoctoral Fellow, Materials Science and Engineering
PhD, Stanford, 2015
Cui Lab: When the size of materials is reduced to the nanoscale dimension, physical and chemical properties can change dramatically. In addition, nanostructures also afford new exciting opportunities of low-cost processing. We are interested in a broad range of nanoscale properties including electronic, photonic, electrochemical, mechanical, catalytic and interfacial properties. Understanding these properties has important technological implications in energy conversion and storage, electronics, biotechnology and environmental technology. We study fundamentals of nanomaterials including nanowires, colloidal nanocrystals and patterned nanostructures, develop low-cost processings and address critical issues in real-world applications.
News Release 8/15/16: SLAC, Stanford Gadget Grabs More Solar Energy to Disinfect Water Faster
h-index: 20 Total Citations: 1252 (Google Scholar Citations, Dec. 2017)
Faculty Recruiting Seminar
Wednesday, January 10, 3:30pm - 4:30pm, WEL 2.122
Postdoctoral Fellow, Center for Bio-Inspired Energy Research
PhD, Weizmann Institute, Israel, 2013
My current work focuses on ratchets – far-from-equilibrium devices that transport particles using local asymmetries, rather than overall biases. Ratchets are rectifiers – they extract directional motion from non-directed sources of energy, like chemical energy and Brownian motion. Biological motors in the body use ratchet mechanisms, and produce motion very efficiently, even in the highly-damped biological conditions, where the noise is actually orders of magnitude stronger than the chemical energy available. We want to understand how the ratcheting applies to electrons, especially under highly-damped conditions, like in low-mobility organic semiconductors. Very little experimental work has been done on electron ratchets, and so we mainly seek to improve our understanding of the mechanism, with an eye toward possible future applications in solar cells or other electronic devices.
h-index: 5 Total Publications: 14 Total Citations: 165 (ResearcherID, Nov. 2017)
h-index: 5 Total Citations: 212 (Google Scholar Citations, Nov. 2017)
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