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Professor Stenner

Reinhard Schweitzer-Stenner, PhD

Department of Chemistry
Office: Disque Hall 605a
Phone: 215.895.2268
Fax: 215.895.1399

Additional Sites:


  • MS,  Physics, Bergische Universität Wuppertal (Germany), 1980
  • Dr rer nat, Physics, Universität Bremen (Germany), 1983
  • Venia Legendi (Habilitation), Experimental Physics, Universität Bremen, 1990

Research Interests:

Vibrational Spectroscopy, with an emphasis on Raman and resonance Raman spectroscopy; structure analysis of peptides in solution; understanding the coil state of peptides and proteins; protein folding of Heme proteins (cytochrome c, myoglobin, horseradish peroxidase), particularly the relationship between heme-protein interactions and function; theoretical modeling of ligand-receptor interactions and transmembrane signaling in mast cells.

Selected Publications:

Most Recent Publications (2015-2014)

Conformational Analysis of Short Peptides

  • R. Schweitzer-Stenner, H. Carson and D. DiGuiseppi. Probing the Replacement of Water by Dimethyl Sulfoxide in the Hydration Shell of N-Methylacetamide by FTIR Spectrosocopy. Vib. Spectrosc. 2017, 92, 251-258.
  • D. DiGuiseppi, B. Milorey, G. Lewis, N. Kubatova, S. Farrell, H. Schwalbe and R. Schweitzer-Stenner. Probing the Conformation-Dependent Preferential Binding of Ethanol to Cationic Glycylalanylglycine in Water/Ethanol by Vibrational and NMR Spectroscopy . J. Phys. Chem. B. 2017, 121, 5744-5758.
  • D. DiGuiseppi, J. Kraus, S.E. Toal, N. Alvarez and R. Schweitzer-Stenner. Investigating the Formation of a Repulsive Hydrogel of a Cationic 16mer Peptide at Low Ionic Strength in Water by Vibrational Spectroscopy and Rheology. J. Phys. Chem B. 2016, 120, 10079−10090.
  • Schweitzer-Stenner and S.E. Toal. Construction and Comparison of the Statistical Coil States of Unfolded and Intrinsically Disordered Proteins from Nearest-Neighbor Corrected Conformational Propensities of Short Peptides. Mol. BioSys. 2016, 12, 3294-3306.
  • J. Smith, D. Hagarman, D. DiGuiseppi, R. Schweitzer-Stenner and H.-F. Ji. Ultra-Long Crystalline Red Phosphorus Nanowires from Amorphous Red Phosphorus Thin Films. Angew. Chemie (Int. Edition). 2016, 55, 11829-11833.
  • S. Farrell, D. DiGuiseppi, N. Alvarez and R. Schweitzer-Stenner. The interplay of aggregation, fibrillization and gelation of an unexpected low molecular weight gelator: glycylalanylglycine in ethanol/water. Soft Matter. 2016, 12, 6096-6110.
  • D. DiGuiseppi and R. Schweitzer-Stenner. Probing conformational propensities of histidine in different protonation states of the unblocked glycyl-histidyl-glycine peptide by vibrational and NMR spectroscopy. J. Raman Spectrosc. 2016, 47, 1063-1072.
  • D. Meral, S.E. Toal, R. Schweitzer-Stenner and B. Urbanc. Water-Centered Interpretation of Intrinsic pPII Propensities of Amino Acid Residues: In Vitro-Driven Molecular Dynamics Study. J. Phys. Chem. B. 2015,  119, 13237-13251.
  • B. Milorey, S. Farrell, S.E. Toal and R. Schweitzer-Stenner. Demixing of water and ethanol causes conformational redistribution and gelation of the cationic GAG tripeptide. Chem. Comm. 2015, 51, 1698-1650.
  • N.V. Ilawe, A.E. Raeber, R. Schweitzer-Stenner, S.E. Toal, and B.M. Wong. Assessing backbone solvation effects in the conformational propensities of amino acid residues in unfolded peptides. Phys.Chem.Chem.Phys. 2015, 17, 24917-24924.
  • S.E. Toal, N. Kubatova, C.Richter, V. Linhard, H. Schwalbe, and R. Schweitzer-Stenner. Randomizing the Unfolded State of Peptides (and Proteins) by Nearest Neighbor interactions between Unlike Residues. Chem. Eur. J. 21, 5173-5192, 2015 (designated as hot paper by the editor).
  • R. Schweitzer-Stenner and S.E. Toal. Entropy reduction in unfolded peptides (and proteins) due to conformational preferences of amino acid residues. Phys.Chem.Chem.Phys. 2014, 16, 22527-22536.
  • S.E. Toal and R. Schweitzer-Stenner. Local Order in the Unfolded State: Conformational Biases and Nearest Neighbor Interactions. Biomolecules, 2014, 4, 725-773 (invited review).
  • S.E. Toal, D.J. Verbaroand R. Schweitzer-Stenner. Role of Enthalpy−Entropy Compensation Interactions in Determining the Conformational Propensities of Amino Acid Residues in Unfolded Peptides. J. Phys. Chem. B. 2014, 118, 1309-1318.

    Cytochrome c Structure and Function
  • B. Milorey, D. Malyshka and R. Schweitzer-Stenner. pH Dependence of Ferricytochrome c Conformational Transitions During Binding to Cardiolipin Membranes: Evidence for Histidine as the Distal Ligand at Neutral pH. J. Phys. Chem. Lett. 1993-1998, 8, 201.
  • D. Malyshka, and R. Schweitzer-Stenner. Ferrocyanide-mediated Photoreduction of Ferricytochrome c Utilized to Selectively Probe Non-Native Conformation Induced by Binding to Cardiolipin Containing Membranes. Chem. Eur. J2017, 23, 1151-1156.
  • L. Serpas, B. Milorey, L.A. Pandiscia, A.W. Addison, and R. Schweitzer-Stenner. Autoxidation of Reduced Horse Heart Cytochrome c Catalyzed by Cardiolipin-Containing Membranes. J. Phys. Chem. B. 2016, 120, 12219-12231.
  • L. Pandiscia and R. Schweitzer-Stenner. Coexistence of Native-Like and Non-Native Cytochrome c on Anionic Liposomes with Different Cardiolipin Content. J. Phys. Chem. B. 2015, 119, 12846-12859.
  • L. A. Pandiscia and R. Schweitzer-Stenner. Coexistence of Native-like and Non-Native Partially Unfolded Ferricytochrome c on the Surface of Cardiolipin-Containing. J. Phys. Chem. B. 2015, 119, 1334-1349.
  • D. Malyshka, L.A. Pandiscia and R. Schweitzer-Stenner. Cardiolipin containing liposomes are fully ionized at physiological pH. An FT-IR study of phosphate group ionization. Vibr. Spectrosc. 2014, 75, 86-92.
  • R. Schweitzer-Stenner. Cytochrome c: A Multifunctional Protein Combining Conformational Rigidity with Flexibility. New J. Sci., 2014 (invited review).
  • L. A. Pandiscia and R. Schweitzer-Stenner. Salt as a catalyst in the mitochondria: returning cytochrome c to its native state after it misfolds on the surface of cardiolipin containing membranes. Chem. Comm. 2014, 50, 3674-3676.