Chemical Physics and Physical Chemistry

Donald D. Fitts

First Name: 
Donald D.
Last Name: 
Official Title: 
Emeritus Professor of Chemistry

Physical Chemistry

Contact Information
Office Location: 
Senior Faculty Suite
(215) 898-8628
  • A.B. Harvard University (1954)
  • Ph.D. Yale University (1957)
  • N.S.F. Postdoctoral Fellow, University of Amsterdam (1957-58)
  • NATO Senior Science Fellow, Imperial College, University of London (1971)
  • Academic Visitor, Oxford University (1978)
  • Associate Dean for Graduate Studies, School of Arts and Sciences (1978-82, 83-94)
  • Acting Dean, School of Arts and Sciences (1982-83)
  • Visiting Fellow, Corpus Christi College, Cambridge and Visiting Scholar, Department of Chemistry, University of Cambridge, U.K. (1996)
Research Interests: 

From a knowledge of the interactions among molecules, it is possible in principle to predict the structure and the thermodynamic properties of materials as well as the dynamics of molecular processes. The overall objective of our research program is twofold: to evaluate the potential energies of intermolecular interactions for various systems as accurately as possible and to study by means of statistical mechanics the influence of these potentials of intermolecular force on the structure and properties of macroscopic systems.

Zahra Fakhraai

First Name: 
Last Name: 
Official Title: 
Associate Professor of Chemistry

Physical Chemistry, Materials Chemistry, Nanoscale Science and Engineering

Contact Information
Admin Support: 
  • B.Sc. Physics, Sharif University of Technology, Iran 1999
  • M. Sc. Physics, Sharif University of Technology, Iran 2001
  • Ph.D. Physics, University of Waterloo, 2007
  • Post-Doctoral associate, Chemistry, University of Toronto, 2007-08.
  • NSERC Post-Doctoral Fellow, Chemistry, University of Wisconsin-Madison, 2009-11.
Research Interests: 

Our group is interested to study the effect of nano-confinement on structure, dynamics and other properties of materials. Materials behave differently on surfaces, interfaces or small length scales compared to their bulk properties.  Understanding such differences are crucial in many technological applications where materials are constrained in nanometer size spaces, such as organic electronics, polymer applications and drug delivery. One can take advantage of such difference to produce novel materials, such asexceptionally stable glasses or harvest light for various applications. In biological systems, most of the dynamics happens in nanometer size proximity of surfaces and interfaces, and understanding the properties in confinement is a key in predicting function. We focus our efforts on understanding the origins of such modified properties on a fundamental level as well as possible application of such phenomena in producing novel materials or experimental tools.

Enhanced Mobility at the Surface of Polymeric and Organic Glasses: 


We study the properties of glasses at the air/glass interface. Our studies show that below the glass transition temperature, where the bulk of the material is in an out of equilibrium state, the interfacial dynamics are many orders of magnitude faster that the bulk dynamics. As a result a layer close to the interface maintains equilibrium properties. We study the dynamics of this layer, its thickness, and its effect on the properties of the underlying glass. The interfacial layer can strongly modify properties of amorphous materials in nanometer length scales. They also allow one to produce near-equilibrium structures at temperatures well below bulk glass transition temperature, through physical vapor deposition.

Exceptionally Stable Glasses: 


The enhanced mobility of the interfacial layer allows us to produce near-equilibrium glasses at temperatures well below the bulk glass transition temperature, Tg, by means of physical vapor deposition (PVD). Exceptionally stable glasses are formed when the substrate temperature during PVD is maintained just below the glass transition temperature. We study the morphology and the kinetics of PVD films during formation and their relationship to the final properties of the stable glass. These studies provide information on mechanisms of rapid aging below Tg and stable glass formation. We also investigate exceptional material properties of these glasses and the role of the chemical structure in these properties such as the optical birefringence and electronic properties.


Novel Emergent Optical Properties in Disordered Nanoparticle Clusters: 


Using simple synthetic routs we can produce dielectric core-gold shell nanoparticles decorated with randomly packed nanoparticles of various shapes and sizes. Spiky nanoparticles are a good example of such nanoparticles. Broadband and tunable structure of spiky gold nanoshells makes them ideal for various applications such as enhanced Raman scattering, temperature and index sensing and sensors for biological and light harvesting applications. Exceptional properties, such as higher order quadrupoloar scattering and magnetic dipole plasmons in these nanoparticles are due to inherent disorder in their structure and random packing arrangements. We explore optical properties of these nanoshells, using various theoretical and experimental tools. We also develop new techniques that allow us to study properties of meta materials formed from these types of particles.


Surface Mediated Self-assembly of Amyloid Aggregrates: 


Surface self-assembly provides an alternative pathway for amyloid aggregation that is not available in bulk solutions. We us high-resolution atomic force microscopy and other imaging techniques to study the adhesion and diffusion of peptides on various surfaces and their role in facilitating amyloid fibril formation through self-assembly routs. We also use our exceptional capabilities in high-resolution imaging to study the conformation of amyloids formed under various conditions in aqueous conditions.

Selected Publications: 

1.     T. Liu, K. Cheng, E. Salami, F. Gao, C. Li, X. Tong, Y. Lin, Y. Zhang, W. Zhang, L. Klinge, P. Walsh and Z. Fakhraai, "The effect of chemical structure on the stability of physical vapor deposited glasses of 1,3,5-triarylbenzene"J. Chem. Phys. 143, 084506 (2015). 

2.     Z. Qian, S.P. Hastings, C. Li, B. Edward, C.K. McGinn, N. Engheta, Z. Fakhraai* and S.J. Park, "Raspberry-like Metamolecules Exhibiting Strong Magnetic Resonances",  ACS Nano9, 1263-1270 (2015). 

3.     E. Glor, and Z. Fakhraai, "Facilitation of Interfacial Dynamics in Entangled Polymer Films", J. Chem. Phys. 141, 194505 (2014).

4.     Y. Lin, E.J. Peterson, and Z. Fakhraai, "Surface Effects Mediate Self-Assembly of Amyloid-β Peptides"ACS Nano8, 10178-10186 (2014).

5.     S. P. Hastings, P. Swanglap, Z. Qian, Y. Fang, S.J. Park, S. Link, N. Engheta, and Z. Fakhraai, "Quadrupole-Enhanced Raman Scattering", ACS Nano,  8 , 9025-9034 (2014).

6.     B. Sanchez-Gaytan, Z. Qian, S. Hastings, M. Reca, Z. Fakhraai, and S. J. Park, “Controlling
the Topography and Surface Plasmon Resonance of Gold Nanoshells by a Templated Surfactant-Assisted Seed Growth Method
 ”, J. Phys. Chem. C. 117, 8916-8923 (2013).

7.     C. R. Daley, Z. Fakhraai, M. D. Ediger, and J. A. Forrest, “Comparing Surface and Bulk Flow of a Molecular Glass Former”, Soft Matter, 8, 2206-2212 (2012). 

8.     M. Paulite, Z. Fakhraai, N. Gunari, A. Tanur, and G. C. Walker, “Imaging Secondary Structure of Individual Amyloid Fibrils of a β(2)-Microglobulin Fragment Using Near-Field Infrared Spectroscopy”, J. Am. Chem. Soc. 133, 7376-7383 (2011).

9.     Z. Fakhraai and J. A. Forrest, “Measuring the Surface Dynamics of Glassy Polymers”, Science, 319, 600- 604 (2008).

10.  Z. Fakhraai, and J. A. Forrest, “Probing Slow Dynamics in Supported Thin Polymer Films”, Phys. Rev. Lett. 95, 025701(2005).

Ivan J. Dmochowski

First Name: 
Ivan J.
Last Name: 
Official Title: 
Professor of Chemistry

Bioinorganic, Bioorganic, Biophysical Chemistry

Additional Titles: 
Undergraduate Chair
Contact Information
Office Location: 
348 N, Lab: 332, 334, 336, 338 N
Admin Support: 
  • B.A. Harvard College (1994)
  • Research Fellow, Johannes Gutenberg Universitaet, Mainz, DE (1994-1995)
  • Ph.D. California Institute of Technology (2000)
  • Caltech Herbert Newby McCoy Award (2000)
  • Helen Hay Whitney Postdoctoral Fellow, Biophysics, Caltech (2000-2002)
  • Camille and Henry Dreyfus New Faculty Award (2003)
  • National Science Foundation CAREER Award (2005)
  • Camille and Henry Dreyfus Teacher-Scholar Award (2007)
Research Interests: 

Our lab is developing chemical and biophysical tools to study and manipulate complex biological systems. Projects span many areas of synthetic organic, inorganic, and biophysical chemistry; molecular, cell, and developmental biology; and bioengineering. We are particularly interested in developing new technologies for biomolecular imaging and the fabrication of functional bio-nanomaterials.

Hyperpolarized 129Xe Biosensors for Early Cancer Detection

Molecular imaging technologies hold great promise for early cancer diagnosis and intervention. Our goal is to develop new reagents that extend the capabilities of magnetic resonance imaging (MRI) for monitoring multiple cancer markers simultaneously in vivo. 129Xe has found increasing use for biological imaging applications, due to its biological compatibility (xenon is an anesthetic at high concentrations), hyperpolarizability (this enhances signals 1,000-fold), and high affinity for organic cages such as cryptophanes. The chemical shift of 129Xe varies by a remarkable 200 ppm, depending on its molecular environment: Thus, a 129Xe atom encapsulated inside a cryptophane is a sensitive reporter of perturbations outside the cage. Based on this principle, our lab is generating new biosensors that will identify biomarkers associated with cancers of the breast, lungs, brain, and pancreas. The long-range goal of this project is to use MRI to detect aberrant proteins that cause cancer in humans, years before the formation of a tumor.

Ferritin Templates for Nanoparticle Synthesis and Assembly

The goal of this project is to use ferritin proteins as templates for synthesizing and assembling inorganic nanoparticles with nanometer precision. Ferritins contain 24 four-helix bundle subunits that self-assemble to create a large central cavity. We have made water-stable, 10-12-nm gold and silver nanoparticles inside ferritin (gray sphere). Particles are fully characterized using facilities at the UPenn Laboratory for Research on the Structure of Matter (LRSM). We are functionalizing the surface of these ferritin-metal nanoparticles for sensing and nano/biomaterials applications. We are also performing computational protein design, in collaboration with the Saven lab, to mutate residues inside the ferritin cavity to enhance their metal-binding properties. Methods for organizing ferritin metal nanoparticles in 2- and 3-dimensions are being developed, in order to build very small conducting circuits. 

Laser-Activated Chemical Biology: Controlling Genes with Light

The goal of this project is to develop methods for turning genes "on" and "off" with light inside neurons and developing zebrafish embryos with high spatial and temporal control. As a first step, we have developed methods for incorporating a photoactive blocking group in the middle of a DNA or RNA oligonucleotide. In one application, we modulated primer extension by DNA polymerase (KF) using UV light. Photoactivation was monitored using a fluorescent reporter. We are now developing methods to control protein translation by the ribosome using similarly caged RNA. Blocking groups mask the messenger RNA start codon, and are designed to prevent translation until photocleavage. We will control complex gradients of proteins involved in cell signaling during zebrafish development and wound healing, using a state-of-the-art UV confocal microscope in the lab.

Selected Publications: 


X. Tang, J. Swaminathin, A.M. Gewirtz, I.J. Dmochowski, Regulating gene expression in human leukemia cells using light-activated oligodeoxynucleotides, Nucl. Acids Res. (36) 559-569, 2008.


J.A. Aaron, J.M. Chambers, K.M. Jude, L. Di Costanzo, I.J. Dmochowski, D.W. Christianson, Structure of a 129Xe-cryptophane biosensor complexed with human carbonic anhydrase II, J. Am. Chem. Soc. (130) 6942-6943, 2008.


G.K. Seward, Q. Wei, I.J. Dmochowski, Peptide-mediated cellular uptake of cryptophane, Bioconjug. Chem. (19) 2129-2135, 2008.


J.L. Richards, X. Tang, A. Turetsky, I.J. Dmochowski, RNA bandages for photomodulating in vitro protein synthesis, Bioorg. Med. Chem. Lett. (18) 6255-6258, 2008.


C. Butts, J. Swift, S.-G. Kang, L. Di Costanzo, D.W. Christianson, J.G. Saven, I.J. Dmochowski, Directing noble metal ion chemistry within a designed ferritin protein, Biochemistry (47) 12729-12739, 2008.


J.L. Chambers, P.A. Hill, J.A. Aaron, Z. Han, D.W. Christianson, N.N. Kuzma, I.J. Dmochowski, Cryptophane xenon-129 nuclear magnetic resonance biosensors targeting human carbonic anhydrase, J. Am. Chem. Soc. (131) 563-569, 2009.


P.A. Hill, Q. Wei, T. Troxler, I.J. Dmochowski, Substituent effects on xenon binding affinity and solution behavior of water-soluble cryptophanes, J. Am. Chem. Soc. (131) 3069-3077, 2009.


G.P. Robbins, M. Jimbo, J. Swift, M.J. Therien, D.A. Hammer, I.J. Dmochowski, Photo-initiated destruction of composite porphyrin-protein polymersomes, J. Am. Chem. Soc., (131) 3872-3874, 2009. 


J. Swift, C. Butts, J. Cheung-Lau, V. Yerubandi, I.J. Dmochowski, Efficient self-assembly of Archaeoglobus fulgidus ferritin around metallic cores, Langmuir, (25) 5219-5225, 2009.


C.A. Butts, J. Xi, G. Brannigan, M.L. Klein, R.G. Eckenhoff, I.J. Dmochowski, Identification of a fluorescent general anesthetic, 1-aminoanthracene, Proc. Natl. Acad. Sci. U.S.A. (106) 6501-6506, 2009.


I.J. Dmochowski, Xenon out of its shell, Nature Chemistry, ‘In Your Element’ invited feature article, vol. 1, 250, June 2009.


O. Taratula, I.J. Dmochowski, Functionalized 129Xe contrast agents for magnetic resonance imaging, Curr. Opin. Chem. Biol. (14) 97-104, 2010.


J.L. Richards, G.K. Seward, Y. Huang, I.J. Dmochowski, Turning DNAzymes on and off with light, ChemBioChem (11) 320-324, 2010.


J. Lampe, Z. Liao, I.J. Dmochowski, P.S. Ayyaswamy, D.M. Eckmann, Imaging macromolecular interactions at an interface, Langmuir (26) 2452-2459, 2010.

Courses Taught: 
  • Chemistry 101, "General Chemistry"
  • Chemistry 559, "Biomolecular Imaging"
  • Chemistry 567, “Bioinorganic Chemistry”

J. Kent Blasie

First Name: 
J. Kent
Last Name: 
Official Title: 
Walter H. & Leonore C. Annenberg Professor in the Natural Sciences

Biological, Chemical Physics and Physical Chemistry

Contact Information
Office Location: 
2003 Vagelos, Lab: Vagelos 2170, 2190, 2210-2211, 2230-2231 and 2240
(215) 898-6208
  • B.S. University of Michigan (1964)
  • Ph.D. University of Michigan (1968)
  • USPHS Career Development Award (1971-76)
  • Guest Biophysicist, Brookhaven National Laboratory (1973-present)
  • Chairman, Department of Chemistry (1983-1986)
  • Director, Biostructures Participating Research Team, National Synchrotron Light Source, Brookhaven National Laboratory (1985-1994)
  • Executive Committee, Complex Materials Collaborative Access Team, Advanced Photon Source, Argonne National Laboratory (1994-present)
  • Scientific Advisory Committee & Advisory Board, Spallation Neutron Source, Oak Ridge National Laboratory (1997-2006)
  • Executive Committee, Cold Neutrons in Biology and Technology Team, National Institutes of Standards and Technology (1998-2006)
  • Director, Complex Materials Collaborative Access Team, Advanced Photon Source, Argonne National Laboratory (2001-present)
Research Interests: 

Our research program falls into two areas, namely nano-scale materials science and fundamental biophysics (or biophysical chemistry). The materials science effort is directed toward the development of novel electro-optical devices, both single particle and 2-D to 3-D ensemble based, utilizing the unique microscopic properties of designed cofactor-artificial peptide complexes. The cofactors are based primarily on extended conjugated chromophores designed to exhibit light-induced electric charge transfer over large nano-scale distances and possess minimal HOMO-LUMO bandgaps. The highly stable, artificial α-helical peptides are based on n-helix bundle structural motifs designed to vectorially incorporate the cofactor within the core of the bundle and to order the assembly of the peptide-cofactor complexes at the liquid-gas, solid-liquid or solid-gas interface. Ensembles of these complexes have potential for both photovoltaic devices applications relevant to solar energy conversion and non-linear optical device applications relevant to broad-band communications. The structures and properties of both the isolated complexes and the ensembles thereof are determined by cutting-edge techniques, including molecular dynamics simulation, synchrotron x-ray and cold neutron scattering, and polarized CW and transient spectroscopies. The biophysics effort is directed toward understanding the mechanism of volatile general anesthetic action on membrane ion channels. To better access the physical chemistry of the anesthetic-protein interaction, we are utilizing artificial membrane ion channels based on an amphiphilic 4-helix bundle motif, the hydrophilic domain designed to possess the anesthetic binding cavity and the hydrophobic domain designed as a membrane-spanning cation channel. The same techniques mentioned above are utilized to probe the nature of the anesthetic-peptide interaction and its effect on the conformation of the ion channel domain. Future work will also be directed toward understanding the mechanism of electro-mechanical coupling in the substantially more complex, natural voltage-gated ion channels under the control of the applied transmembrane electrochemical potential. These studies will employ cutting-edge time-resolved synchrotron x-ray and cold neutron scattering techniques coupled with molecular dynamics simulation, and will lead to the investigation of the effects of anesthetic binding on this mechanism. All of the work mentioned above involves both extensive collaborations with other faculty in the Department, at Penn, and elsewhere, as well as experimental work at the National Laboratories on a regular basis.

Figure Legend #1: An instantaneous configuration from a molecular dynamics simulation of the structure of an extended conjugated chromophore (a butadiyne-bridged Zn-porphyrin dimer: red/yellow) incorporated into the core of the hydrophilic domain of an amphiphilic 4-helix bundle peptide (green ribbon representation) and vectorially-oriented at the water-octane (gray-pink) interface. The time-averaged structure of the chromophore-peptide complex within a monolayer ensemble at the interface has been determined experimentally. The designed coiled-coil structure of the 4-helix bundle induces a twist in the chromophore that is key to optimizing its non-linear optical polarizability.

Figure Legend #2: Instantaneous configurations from molecular dynamics simulations of the structures of a computationally designed, model anesthetic-binding membrane ion channel vectorially-oriented at the water-octane interface (water/octane not shown; see Figure 1). The hydrophilic domain (blue ribbon representation) of the amphiphilic 4-helix bundle peptide contains the anesthetic-binding cavity with the volatile anesthetic halothane (CPK representation) in the cavity shown on the right-side, with the ion channel hydrophobic domain (red ribbon representation). The helices are relatively straight and un-coiled in the side-on view (upper), as more readily seen in the end-on view shown below. Removal of the anesthetic from the cavity is seen to induce a coiled-coil structure extending from the cavity into the ion channel hydrophobic domain, shown in the side-on and end-on views on the left side. Importantly, this anesthetic-dependent conformational change depends upon the amino acid composition of the cavity. Experimental verification of these predictions from the computational design and molecular dynamics simulations are underway.

Selected Publications: 


Gupta, S., Dura, J., Freites, A. Tobias, D. and Blasie, J.K. Structural characterization of the voltage sensor domain and voltage-gated K+-channel vectorially-oriented within a single bilayer membrane at the solid/vapor and solid/liquid interfaces via neutron interferometry. Submitted.


Koo, J., Park, J., Tronin, A., Zhang, R., Krishnan, V., Strzalka, J., Kuzmenko, I., Therien, M.J. and Blasie, J.K. Acentric 2-D Ensembles of D-br-A Electron-Transfer Chromophores via Vectorial Orientation within Amphiphilic n-Helix Bundle Peptides for Photovoltaic Device Applications. Langmuir, 28: (6), pp 3227-3238 


Gupta, S., Liu, J., Strzalka, J. and Blasie, J.K. (2011) Profile Structures of the VSD and KvAP Channel Vectorially-Oriented in Single Membranes at Solid-Vapor or Solid-Liquid Interfaces via X-ray Reflectivity. Phys. Rev. E. 84(3): 031911-1-15.


Korendovych, I., Senes, A., Kim, Y.H., Lear, J., Fry, H.C., Therien, M.J., Blasie, J.K., Walker, F.A. and DeGrado, W.F. (2010) De Novo Design and Molecular Assembly of a Transmembrane Diporphyrin-Binding Protein Complex. J. Am. Chem. Soc. Comm. 132: 15516-15518.


Gonella, G., Dai, H.-L., Fry, H. C., Therien, M. J., Krishnan, V., Tronin, A. and Blasie, J.K. (2010) Control of the Orientational Order and Nonlinear Optical Response of the "Push-Pull" Chromophore RuPZn via Specific Incorporation into Densely-Packed Monolayer Ensembles of an Amphiphilic 4-Helix Bundle Peptide: Second Harmonic Generation at High Chromophore Densities. J. Am. Chem. Soc. 132 (28): 9693–9700. (28) 


Krishnan, V., Tronin, A., Strzalka, J., Fry, H.C., Therien, M.J. and Blasie, J.K. (2010) Control of the Orientational Order and Nonlinear Optical Response of the “Push-Pull” Chromophore RuPZn via Specific Incorporation into Densely-Packed Monolayer Ensembles of an Amphiphilic 4-Helix Bundle Peptide: Characterization of the Cofactor-Peptide Complex in Monolayer Ensembles. J. Am. Chem. Soc. 132(32):11083-11092. (32) 


Krishnan, V., Strzalka, J., Liu, J., Liu, C., Kuzmenko, I., Gog, T. and Blasie, J.K. (2010) Interferometric Enhancement of X-ray Reflectivity from Unperturbed Langmuir Monolayers of Amphiphiles at the Liquid-Gas Interface. Phys. Rev. E 81: 021604-1-10. 


Zou, H. Liu, J. and Blasie, J.K. (2009) Mechanism of interaction between the volatile anesthetic halothane and a model ion channel protein: III. Molecular dynamics simulation incorporating a cyano-phenylalanine spectroscopic probe. Biophys. J. 96(10) pp. 4188 – 4199.



Liu, J., Strzalka, J., Tronin, A., Johansson, J.S. and Blasie, J.K. (2009) Mechanism of interaction between the volatile anesthetic halothane and a model ion channel protein: II. Fluorescence & vibrational spectroscopy employing a cyano-phenylalanine probe. Biophys. J. 96(10) pp. 4176 – 4187.



Strzalka, J., Liu, J., Tronin, A., Johansson, J.S. and Blasie, J.K. (2009) Mechanism of interaction between the volatile anesthetic halothane and a model ion channel protein: I. Structural investigations via x-ray reflectivity from Langmuir monolayers. Biophys. J. 96(10) pp. 4164 – 4175.



Tronin, A., Krishnan, V., Strzalka, J., Kuzmenko, I., Gog, T., Fry, C., Therien, M.J. and Blasie, J.K. (2009) Portable UV-VIS spectrometer for measuring absorbance and dichroism of Langmuir monolayers. Rev. Sci. Instru. 80(3): 033102-1-7.


Zou, H., Therein, M.J. and Blasie, J.K. Structure & Dynamics of an Extended Conjugated NLO Chromophore within an Amphiphilic 4-Helix Bundle Peptide by Molecular Dynamics Simulation. Submitted to J. Phys. Chem. B.


McAllister, K.A., Zou, H., Cockran, F.V., Bender, G.M., Senes, A., Fry, C.F., Nanda, V., Keenan, P.A., Lear, J.D., Therien, M.J., Blasie, J.K, and DeGrado, W.F. Using α-Helical Coiled-Coils to Design Nanostructured Metalloporphyrin Arrays. Submitted to Angewandte Chemie.


Bender, G.M., Lehmann, A., Zou, H., Cheng, H., Fry, H.C., Engel, D., Therien, M.J., Blasie, J.K., Roder, H., Saven, J.G. and DeGrado, W.F. De Novo Design of a Single Chain Diphenylporphyrin Metalloprotein. J. Am. Chem. Soc. 129(35).


Zou, H., Strzalka, J. Xu, T., Tronin, A. and Blasie, J.K. (2007) 3-D Structure and Dynamics via Molecular Dynamics Simulation of a de novo Designed, Amphiphilic Heme Protein Maquette at Soft Interfaces. Phys. Chem. B 111: 1823-1833.


Strzalka, J., Xu, T., Tronin, A., Wu, S.P., Miloradovic, I., Kuzmenko, I. Gog, T., Therien, M.J., and Blasie, J.K. (2006) Structural Studies of Amphiphilic 4-helix Bundle Peptides Incorporating Designed Extended Chromophores for Nonlinear Optical Biomolecular Materials. Nano Lett. 6(11): 2395-2405.


Xu, T., Wu, S.P., Miloradovic, I., Therien, M.J., and Blasie, J.K. (2006) Incorporation of Designed Extended Chromophores into Amphiphilic 4-helix Bundle Peptides for Nonlinear Optical Biomolecular Materials. Nano Lett. 6(11):


Nordgren, C.E., Strzalka, J.W. and Blasie, J.K (2005) Structure of α-Helical Bundle Peptides Vectorially-Oriented at Soft Interfaces via Molecular Dynamics Simulations and X-ray/Neutron Scattering. Submitted to Langmuir.


Churbanova, I., Tronin, A., Strzalka, J.W., Gog, T., Kuzmenko, I., Johansson, J.S. and Blasie, J.K. (2006) Monolayers of a Model Anesthetic-Binding Membrane Protein: Formation, Characterization and Halothane-Binding Affinity. Biophys. J. 90: 3255-3266.


Tronin, A., Xu, T. and Blasie, J.K. (2005) In situ Determination of Orientational Distributions in Langmuir Monolayers by Total Internal Reflection Fluorescence. Langmuir 21: 7760-7767.



Discher, B.M., Noy, D., Strazalka, J, Ye, S., Moser, C.C., Lear, J.D., Blasie, J.K. and Dutton, P.L. (2005) Design of Amphiphilic Protein Maquettes: Controlling Assembly, Membrane Insertion, and Cofactor Interactions. Biochemistry 44:12329-12343.


Ye, S., Discher, B.M., Strzalka, J.W., Xu, T., Wu, S.P., Noy, D., Kuzmenko, I., Gog, T., Therien, M.J., Dutton, P.L. and Blasie, J.K. (2005) Amphiphilic 4-Helix Bundles Designed for Light-Induced Electron Transfer Across Soft Interfaces. Nano Lett. 5(9):1658-1667.


Ye, S., Strzalka, J., Churbanova, I.Y., Zheng, S,, Johansson, J.S. and Blasie JK. (2004) A Model Membrane Protein for Binding Volatile Anesthetics. Biophys. J. 87: 4065-4074.


Strzalka, J. DiMasi, E., Kuzmenko, I., Gog, T. and Blasie, J.K. (2004) Resonant X-ray Reflectivity from a Bromine-Labeled Fatty-Acid Langmuir Monolayer. Phys. Rev. E 70: 051603-1-5.


Strzalka, J., Kneller, L.R., Gibney, B.R., Satija, S., Majkrzak, C.F. and Blasie, J.K. (2004) Specular Neutron Reflectivity and Structure of Artificial Protein Maquettes Vectorially Oriented at Interfaces. Phys. Rev. E. E 70: 061905-1-10. 


Ye, S., Discher, B.M., Strzalka, J.W., Noy, D., Zheng, S., Dutton, P.L. and Blasie, J.K. (2004) Amphiphilic 4-Helix Bundles Designed for BioMolecular Materials Applications. Langmuir 20(14): 5897-5904.


Blasie, J.K., Strzalka, J. and Zheng, S. (2003) Solution to the Phase Problem for Specular X-ray & Neutron Reflectivity from Thin Films on Liquid Surfaces. Phys. Rev. B 67: 224201-1--224201-8.


Ye, S., Strzalka, J., Chen, X., Moser, C.C., Dutton, P.L. and Blasie, J.K. (2003) Assembly of a Vectorially-Oriented Four-Helix Bundle at the Air/Water Interface via Directed Electrostatic Interactions. Langmuir 19(5): 1515-1521.



Zheng, S., Strzalka, J., Jones, D.H., Opella, S.J. and Blasie, J.K. (2003) Comparative Structural Studies of Vpu Peptides in Phospholipid Monolayers by X-ray Scattering. Biophys. J. 84(4): 2393-2415. 84 


Lopez, C. F., Montal, M., Blasie, J.K., Klein, M.L. and Moore, P.B. (2002) Molecular Dynamics Investigation of Membrane-Bound Bundles of the Channel Forming Transmembrane Domain of Viral Protein U from the Human Immunodeficiency Virus HIV. Biophys. J. 83(3): 1259-1267.

http://biophysj/ Volume83


Nordgren, E., Tobias, D.J., Klein, M.L. and Blasie, J.K. (2002) Molecular Dynamics Simulations of a Hydrated Protein Vectorially-Oriented at Hydrophobic vs. Hydrophilic Soft Surfaces. Biophys. J. 83(6): 2906-2917.


Tronin, A., Edwards, A.M., Wright, W.W., Vanderkooi, J.M. and Blasie, J.K. (2002) Orientational Distributions for Cytochrome c on Polar & Nonpolar Soft Surfaces by Polarized Total Internal Reflection Fluorescence. Biophys. J. 82: 996-1003.


Haas, A.S., Pilloud, D.L., Reddy, K.S., Babcock, G.T., Moser, C.C., Blasie, J.K. and Dutton, P.L. Cytochrome c and Cytochrome c Oxidase: Monolayer Assemblies and Catalysis. (2001) J. Phys. Chem. B 105(45): 11351-11362.




Tronin, A. and Blasie, J.K. Variable Acquisition Angle Total Internal Reflection Fluorescence – a New Technique for Orientation Distribution Studies of Ultrathin Films. (2001) Langmuir 17(No. 12): 3696-3703.


Tronin, A., Strzalka, J., Chen, X., Dutton, P.L., Ocko, B.M. and Blasie, J.K. (2001) Orientational Distributions of the Di-α-Helical Synthetic Peptide ZnPPIX-BBC16 by X-ray Reflectivity and Polarized Epifluorescence. Langmuir 17(10): 3061-3066.


Zheng, S., Strzalka, J., Ma, C., Opella, S.J., Ocko, B.M. and Blasie, J.K. (2001) Structural Studies of the HIV-1 Accessory Protein Vpu in Langmuir Monolayers: Synchrotron X-ray Reflectivity. Biophys. J. 80(4): 1837-1850.


Kneller, L.R. , Edwards, A.M., Majkrzak, C.F., Berk, N.F., Krueger, S. and Blasie, J.K. (2001) Hydration State of a Single Cytochrome c Monolayer Vectorially-Oriented at a Soft Interface Investigated via Neutron Interferometry. Biophys. J. 80(5): 2248-2261. 


Strzalka, J., Chen, X., Dutton, P.L. and Blasie, J.K. (2001) X-ray Scattering Studies of Maquette Peptide Monolayers II: Interferometry at the Solid/Vapor Interface. Langmuir 17(4): 1193-1199.


Tronin, A., Strzalka, J., Chen, X., Dutton, P.L. and Blasie, J.K. (2000) Determination of the Porphyrin Orientation Distribution in Langmuir Monolayers by Polarized Epifluorescence. Langmuir 16(25): 9878-9886.


Strzalka, J., Chen, X., Dutton, P.L., Ocko, B. M. and Blasie, J.K. (2000) X-ray Scattering Studies of Maquette Peptide Monolayers I: Reflectivity and GID at the Air/Water Interface. Langmuir 16(26): 10404-10418.


A.M. Edwards, K. Zhang, C.E. Nordgren and J.K. Blasie. (2000) Heme Structure & Orientation in Single Monolayers of Cytochrome c on Polar & Nonpolar Soft Surfaces. Biophys. J. 79: 3105-3117. 79


Blasie, J.K. and Timmins, P. (1999) Neutron Scattering in Structural Biology & BioMolecular Materials in Neutron Scattering in Materials Research, eds. T. Mason and A. Taylor, MRS Bulletin 24(12): 40-47.

Tobias Baumgart

First Name: 
Last Name: 
Official Title: 
Professor of Chemistry

Physical and Biological Chemistry

Additional Titles: 
Graduate Chair
Contact Information
Office Location: 
250 Chemistry Bldg.
Admin Support: 

• Postdoctoral associate with Prof. Watt Webb at Cornell University (2001 – 2005)


• PhD from Max Planck Institute for Polymer Research and Johannes Gutenberg University of Mainz (2001)


• Diploma in Chemistry from the University of Clausthal, Germany (1998)

Research Interests: 

Research in the Baumgart group is largely centered on the physical chemistry of amphiphile membranes with lateral heterogeneity resulting from non-ideal mixing. Our aims include characterization of biologically relevant membranes including lipids and proteins, where we investigate both composition and shape (curvature) heterogeneity. Both of these aspects are thought to be highly relevant to the function of biological membranes. We focus on freely suspended, rather than solid supported membranes, with an emphasis on bilayer membranes, but we also include monolayer systems. We investigate membranes that laterally segregate into co-existing fluid phases, and are particularly interested in quantitatively understanding the phenomenon of line tension at the phase boundary. We also examine molecular details that govern the partitioning of functionally relevant protein constructs between coexisting membrane phases and thereby aim to contribute to enhancing the biophysical understanding of transmembrane signal transduction, particularly in immune cells such as T-cells, B-cells and mast cells. Our research on aspects of membrane shape is directed at understanding how molecules sort in membrane curvature gradients. This curvature sorting likely contributes substantially to intracellular membrane sorting and trafficking. Furthermore we have recently begun to investigate phase coexistence in binary mixtures of amphiphilic di-block copolymers. Finally, we develop methods to pattern cellular signaling ligands, such as antibodies and adhesion molecules, on pattern scales both above and below optical resolution.

Selected Publications: 

31) Heinrich, M., Tian A.,Esposito C., Baumgart T. (2010). Dynamic sorting of lipids and proteins by membrane curvature: a moving phase boundary problem. Proceedings of the National Academy of Sciences. In Print.

30) Johnson, S., Stinson, B., Reminik, J., Go, M., Fang, X., & Baumgart, T. (2010). Temperature dependent phase behavior and protein partitioning in giant plasma membrane vesicles. Biochimica et Biophysica Acta - Biomembranes. In Print.

29) Capraro, B. R., Yoon, Y., Cho, W., Baumgart, T. (2010). Curvature sensing by the epsin N-terminal homology (ENTH) domain measured on cylindrical lipid membrane tethers. Journal of the American Chemical Society, 132 (4), 1200-1201.

28) Levental, I., Byfield, F. J., Choudhourie, P., Madara, J., Gai, F., Baumgart, T., & Janmey P. A. (2009). Cholesterol-dependent phase separation in cell-derived giant plasma membrane vesicles. Biochemical Journal, 424 (2), 163-167.

27) Baker, R. G., Hsu, C. J., Lee, D., Jordan, M. S., Maltzman, J. S., Hammer, D. A., Baumgart, T., & Koretzky, G. A. (2009). The adapter protein SLP-76 mediates “outside-in” integrin signaling and function in T cells. Molecular and Cellular Biology, 29 (20), 5578-5589.

26) Christian, D., Tian, A., Ellenbroek, W., Levental, I., Rajagopal, K., Janmey, P., Liu, A., Baumgart, T., & Discher, D. (2009). Spotted vesicles, striped micelles and Janus assemblies induced by ligand binding. Nature Materials, 8, 843-849. DOI

25) Oh, H., Mohler III, E. R., Tian, A., Baumgart, T., & Diamond, S. L. (2009). Membrane cholesterol is a biomechanical regulator of neutrophil adhesion. Arteriosclerosis, Thrombosis, and Vascular Biology, 29, 1290-1297.

24) Tian, A., Capraro, B. R., Esposito, C., & Baumgart, T. (2009). Bending stiffness depends on curvature of ternary lipid mixture tubular membranes. Biophysical Journal, 97 (6), 1636-1646.

23) Das SL, Jenkins JT, Baumgart T. "Neck geometry and shape transitions in vesicles with co-existing fluid phases: Role of Gaussian curvature stiffness versus spontaneous curvature." Europhysics Letters, 2009, 86, 48003-48008.

22) Tian, A. and Baumgart, T. "Sorting of lipids and proteins in membrane curvature gradients." Biophysical Journal, 2009, 96, 2676-2688.

21) Das S., Tian A., Baumgart T., "Mechanical stability of micropipette aspirated giant vesicles with fluid phase coexistence." Journal of Physical Chemistry, B 2008, 112, 11625-11630.

20) Heinrich M.C., Levental I., Gelman H., Janmey P.A., Baumgart T. "Critical exponents for line tension and dipole density difference from lipid monolayer domain boundary fluctuations." Journal of Physical Chemistry, B 2008, 112, 8063-8068.

Department of Chemistry

231 S. 34 Street, Philadelphia, PA 19104-6323

215.898.8317 voice | 215.573.2112 fax |

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