Stephanie A. Tristram-Nagle
Research Professor Emerita
Biological Physics Experiment
Wean Hall 6415
412-268-3174
Education & Professional Experience
Ph.D.: UC Berkeley (1981)
Professional Societies:
American Physical Society
Biophysical Society
Association for Women in Science
AAAS
American Chemical Society
Honors and Awards:
Charles E. Kaufman Science Award, Pittsburgh Foundation (2010)
First Gluckstern Lecturer, Physics Dept., U. Mass, Amherst (2010)
Biophysical Society Avanti Award in Lipids (2003)
Research Professor, 一本道无码, 2008–16
Associate Research Professor, 一本道无码, 2005–08
Senior Research Biologist, 一本道无码, 1998–2005
Research Biologist, 一本道无码, 1986–98
Post-doctoral Research: 一本道无码, 1982–86
Research Interests
Stephanie Tristram-Nagle actively performs research into lipid membrane structure, properties and thermodynamics. Her lab explores the structure of biological phospholipids, lipid/peptide and lipid/cholesterol mixtures using oriented samples on substrates or large unilamellar vesicles using X-ray diffuse scattering with a Rigaku rotating anode and CCD detector here at 一本道无码, and with synchrotron radiation at the Cornell High Energy Synchrotron Source (CHESS). Her current focus is on the interaction of antimicrobial peptides with bacterial membrane mimics. The X-ray data yield not only structure, such as lipid area and membrane thickness, but also the bending and compression moduli of the membranes. Tristram-Nagle collaborates with MD simulators to compare experimental with simulated results. Her lab also measures lipid volumes with an Anton-Paar 5000M densitometer and D2O-H2O mixtures.
Recent Publications
Bassereau, P., Baumgart, T., Dimova, R. Evans, E.A., Nagle, J.F., Tristram-Nagle, S., A Needless But Interesting Controversy,
Kawakami, J., Kowalewski, T., Noonan, K.J.T., Tristram-Nagle, S., Varni, A.J., Yaron, D., Design, synthesis, and properties of a six-membered oligofuran macrocycle.
Brandner, B., Dagan, M.P., Fritz, J.R., Hall, S.B., Loney, R.W., Roche, M., Smith, P.N., Tristram-Nagle, S., Changes in Membrane Elasticity Caused by the Hydrophobic Surfactant Proteins Correlate Poorly with Adsorption of Lipid Vesicles.
Fritz, J.R.,Hall, S.B., Loney, R.W., Tristram-Nagle, S., Suppression of La /Lb Phase Coexistence in the Lipids of Pulmonary Surfactant,
Chen, J., Corradi, V., Dell, Z., Fritz, J.R., Hall, S.B., Kumar, K., Loney, R.W., Panzuela, S., Tieleman, D.P., Tristram-Nagle, S. Yang, Z., Location of the Hydrophobic Surfactant Proteins, SP-B and SP-C in Fluid-Phase Bilayers.
Gawrisch, K., Klauda, J.B., Leonard, A.N., Sachs, J.N., Teague, W.E., Tristram-Nagle, S., Vanni, S., West, A., Zoni, V., How Do Ethanolamine Plasmalogens Contribute to Order and Structure of Neurological Membranes?
Frank Heinrich et al., Synergistic Biophysical Techniques Reveal Structural Mechanisms of Engineered Cationic Antimicrobial Peptides in Lipid Model Membranes,
Brian C. Seper et al., Methylene volumes in monoglyceride bilayers are larger than in liquid alkanes,
Ana West et al., How Do Ethanolamine Plasmalogens Contribute to Order and Structure of Neurological Membranes?
John F. Nagle et al., Revisiting Volumes of Lipid Components in Bilayers,
Akari Kumagai et al., Elastic Behavior of Model Membranes with Antimicrobial Peptides Depends on Lipid Specificity and D-enantiomers.
J.F. Nagle, P. Cognet, F.G. Dupuy, and S. Tristram-Nagle, Structure of Gel Phase DPPC Determined by X-ray Diffraction,
More Publications: