Spectroscopy Society of Pittsburgh January Meeting
WHEN: Wednesday – January 16, 2013
WHERE: Duquesne University –
Mellon Hall (Laura Lecture Hall)
RSVP BY: January 11, 2013
TECHNOLOGY FORUM – 5:30PM
George Wunderlich, Executive Director, National Museum of Civil War Medicine
“Medical Advances in the Civil War”
Included in the talk will be discussions involving the scientific advances of the American Civil War including:
Early use of microscopy
Blind studies of new medical treatments
Advances in specialty hospitals and specialized medicine
Advances in medical communications and medical journals
This will all be put in the context of modern practices that find their roots in the Civil War.
George Wunderlich is currently the Executive Director of the National Museum of Civil War Medicine where he formerly held the position of Director of Education. George came to Museum in 2000 after moving from Missouri where he was Founder
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and Director of the Historical Education Center of St. Louis. In 1995 Mr. Wunderlich was awarded the Daughters of the American Revolution National Medal of Honor for his work in public history. After receiving his Master of Arts Degree in American History from Concordia University, he went on to develop new historically-based training programs for the National Park Service, Joint Medical Executive Skills Institute Capstone Symposium, The United State Army Medical Department (AMEDD) and other civilian and government organizations. In October 2011, he was the inducted into the Order of Military
Medical Merit(O2M3) by the AMEDD. He is a nationally known speaker on various Civil War topics and can be regularly seen on the History Channel, A&E, CBS, PBS and the British Broadcasting Corporation.
TECHNICAL PROGRAM – 8:15 PM
Dr. David Clemmer, Indiana University
“Evolution of Protein Structure: From Solution to the Gas Phase”
The structures of macromolecules are often described as native or denatured. While the native state implies a key structural feature that is capable of biological function, much less is implied from the term denatured. In their 1954 paper “Conformations of Proteins”, Lumry and Eyring inferred that the term denatured had “…acquired so many other meanings as to become virtually useless”. In large part, the lack of progress in the last 50 years in understanding non-native structures is the dearth of analytical techniques for probing them. In this talk we describe the development of multidimensional ion mobility spectrometry techniques for following transitions between conformations of macromolecular ions in the gas phase. The approach is to inject a short pulse of ions produced by electrospray ionization into a drift tube containing an inert buffer gas. The distribution of structures separates based on differences in the mobilities. It is possible to select specific states, expose these to energizing collisions, and then follow the new structures that are established by monitoring their mobilities in additional drift tubes. This talk will highlight the
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ubiquitin system. It is possible to
follow many different conformational changes. Recently we have been able to map these gas-phase data back to populations of structures that are present in solution. The ability to follow pathways between structures appears to be useful for refining mobility-based structural assignments. Finally, understanding how structures change will be important for developing next generation mobility instruments that are capable of higher resolving powers.
Professor Clemmer grew up in the southwest where he received a B.S. in Chemistry from Adams State College (1987) and a Ph.D. from the University of Utah (1992). He was a Japan Society for the Promotion of Science Fellow and did postdoctoral work at the Himeji Institute of Technology in Himeji Japan. He continued his postdoctoral work in Martin Jarrold’s laboratory at Northwestern University before joining the Chemistry faculty at Indiana University in 1995. From 2002 to 2006 he served as the chair of the Chemistry Department and he is currently the associate dean for the Natural and Mathematical Sciences.
Clemmer’s research involves the development of analytical methods for studying the structures of complex low-symmetry systems. His group is especially interested in measurements that allow rapid characterization of complex mixtures of biological molecules. Some of the methods have been commercialized and now are being used to address a range of scientific problems, including: elucidation of fundamental issues associated with how proteins fold and aggregate; characterization of the human proteome; and, assessment of molecules that may be used as markers for following specific disease states.
Professor Clemmer’s research group has published more than 175 papers and their work has been recognized with awards from the Sloan, Dreyfus, and National Science Foundations, the American Chemical Society, and the American Society of Mass Spectrometry. He is an
AAAS and FRSC fellow. He was also a member of the Defense Science Study Group.