Kelly Ryan Gallagher
B.Sc., 1990, Boston College
Biochemistry
Ph.D., 2002, University of Pennsylvania
Biochemistry and Molecular Biophysics
Associate Professor
SUNY College at Oneonta
Department of Chemistry & Biochemistry
Oneonta, NY 13820
Office: 227 Physical Science
Research Lab: 242 Physical Science
Telephone: 607-436-3180
kelly.gallagher@oneonta.edu
Courses
Resources for Chemistry in Everyday Life
About Me
Research Interests
My research group focuses on structure-function studies of the human proteins TTC35, COX4 neighbor, and CGI-112. Although their precise cellular role is unknown, these molecules have been identified as components of the ER-associated degradation network (ERAD) and have also been implicated in lipid trafficking. Defects in such pathways have been linked to cystic fibrosis, HIV pathogenicity and several neurodegenerative diseases. We are trying to determine the three dimensional structure of the proteins and determine those components that determine the functional properties of each molecule. Techniques used in the lab include computational modeling of macromolecules, protein purification from recombinant sources, gel electrophoresis, Western blotting, in vitro binding assays, chemical labeling of proteins, and spectroscopy (UV-visible, circular dichroism, protein NMR). We also collaborate with Dr. Nancy Bachman of the Biology Department to create genetic constructs that can be used to produce modified versions of the proteins we study
I also have a strong interest in science outreach/education and teacher education. In my role as Assistant Director of the AJ Read Science Discovery Center of Oneonta, a small interactive science center on the SUNY Oneonta campus, I have been involved in many outreach programs designed to educate the public about both basic science and emerging technologies brought about by recent advances in chemical research. An archive of the "Clued into Nano" activity that we developed for the SDC's 2015 NanoDays event can be downloaded here.
Recent Presentations
“Identification, Cloning, and Characterization of the C-terminal Domain of CGI-112, a Protein Involved in the ER-associated Degradation Pathway.” SUNY Oneonta Life of the Mind, November 2014. (Poster)
“Characterization of the C-terminal Domain of CGI-112, a Protein Involved in the ER-associated Degradation Pathway.” American Chemical Society 249th National Meeting, Division of Biological Chemistry Current Topics in Biochemistry Session, March 2015. (Poster)
“Introduction of the professional quote format and compound screening to project-based experiments in the biochemistry laboratory.” American Chemical Society 249th National Meeting, Chemical Education Division Symposium, Denver, CO, March 2015. (Oral presentation)
“Nanoscience Workshops for Middle School Students- A Collaboration Between the AJ Read Science Discovery Center of Oneonta and The California NanoSystem Institute.” Nanoscale Informal Science Education Network (NISENet) 2015 National Network-wide Meeting, Concurrent Session entitled, “Museum-University Collaborations: Extending Your Collaboration to Other STEM Topics”, St. Paul, MN, June 2015. (Oral presentation)
“Engaging Visitors in Nanoscience via a Life-Sized Clue Game.” NISENet 2015 National Network-wide Meeting, Project Showcase Session, St. Paul, MN, June 2015. (Poster)
Publications
Kelly Gallagher and Kim Sharp. (2003) A New Angle on Heat Capacity Changes in Hydrophobic Solvation. J. Am. Chem. Soc., 125: 9853-60.
Kelly Gallagher and Kim Sharp. (2003) Analysis of Thermal Hysteresis Protein Hydration Using the Random Network Model. Biophysical Chemistry, 105:195-209.
Kelly Gallagher and Kim Sharp. (1998) Electrostatic Contributions to Heat Capacity Changes of DNA-Ligand Binding. Biophysical Journal, 75(2): 769-776.
Kashi Javaherian, Alphonse J. Langlois, David C. Montefiori, Karen A. Kent, Kelly A. Ryan, Peggy D. Wyman, James Stott, Dani P. Bolognesi, Michael Murphey-Corb, and Gregory J. LaRosa. (1994). Studies on the Conformation-Dependent Neutralizing Epitopes of the SIVmac Envelope Protein. J. Virol., 68(4):2624-31.