For a better experience, click the Compatibility Mode icon above to turn off Compatibility Mode, which is only for viewing older websites.

Professor Stenner

Reinhard Schweitzer-Stenner, PhD

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

Additional Sites:
Google Scholar profile


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

Research Interests:

Vibrational Spectroscopy (Infrared, circular dichroism, (resonance) Raman), conformational analysis of peptides in solution; understanding the coil state of peptides and proteins; intrinsically disordered peptides, self-assembly and gelation of low molecular weight peptides, protein folding of heme proteins (cytochrome c, myoglobin, horseradish peroxidase), particularly the relationship between heme-protein interactions and function, cytochrome c - anionic membrane interactions.

Selected Publications:

Most Recent Publications (2022-2019)

Peptide Self-Assembly, Polymers and Gelation

  1. L. J. Thursch, T.A. Thamiresm R. Schweitzer-Stenner and N.J. Alvarez. The impact of thermal history on the structure if glycylalanylglycine ethanol/water gels. J. Pep. Sci. 27, e3305, 2021,
  2. R. Schweitzer-Stenner. The combined use of amide I bands in polarized Raman, IR, and vibrational dichroism spectra for the structure analysis of peptide fibrils and disordered peptides and proteins. Invited review, J. Raman Spectrosc. 52, 2479-2499, 2021,
  3. R. Schweitzer-Stenner and N.J. Alvarez. Short Peptides as Tunable, Switchable, and Strong Gelators. Invited Perspectives article, J. Phys. Chem. B, 125, 6760-6775, 2021,
  4. Levine, M. Gosh, M. Hesser, N. Hennessy, D. DiGuiseppi, L. Adler-Abramovitch, and R. Schweitzer-Stenner. Formation of peptide-based oligomers in dimethylsulfoxide: Identifying the precursor of fibril formation. Soft Matter, 16, 7860-7868,2020, DOI: 10.1039/D0SM00035C
  5. M. Hesser, L. Thursch, T. Lewis, D. DiGuiseppi, N.J. Alvarez, and R. Schweitzer-Stenner. The Tripeptide GHG as Unexpected Hydrogelator Triggered by Imidazole Deprotonation. Soft Matter, 16, 4110-4114, 2020, DOI:10.1039/d0sm00224k.
  6. D. DiGuiseppi, L. Thursch, R. Schweitzer-Stenner and N.J. Alvarez.Exploring the gel phase cationic glycylalanylglycine in water/ethanol. II. Spectroscopic, kinetic and thermodynamic studies. J. Coll. Int. Sci. 573, 123-134, 2020, DOI: 10.1016/j.jcis.2020.03.108.
  7. L. Thursch, D. DiGuiseppi, R. Schweitzer-Stenner and N.J. Alvarez. Exploring the gel phase of cationic glycylalanylglycine in water/ethanol. I. Rheology and Microscopy Studies. J. Coll. Int. Sci., 564, 499-509, 2020. DOI:10.1016/j.jcis.2019.10.029
  8. D. DiGuiseppi, L. Thursch, N. J. Alvarez, and R. Schweitzer-Stenner. Exploring the Thermal Reversibility and Tunability of a Low Molecular Weight Gelator using Vibrational and Electronic Spectroscopy and Rheology. Soft Matter 15, 3418–3431, 2019; DOI: 10.1039/c9sm00104b
  9. J. Pavelec, D. DiGuiseppi, B.Y Zavlavsky, V. N. Uversky and R. Schweitzer-Stenner. Perturbation of water structure by water-polymer interactions probed by FTIR and polarized Raman spectroscopy. J. Mol. Liq. 275, 463-479, 2019;

  10. Conformational Analysis of Unfolded Peptides

  11. R. Schweitzer-Stenner. Exploring Nearest Neighbor Interactions and Their Influence on the Gibbs Energy Landscape of Unfolded Proteins and Peptides. Int. J. Mol. Sci. 23, 5643, 2022,
  12. R.Schweitzer-Stenner, B. Milorey and H. Schwalbe. Randomizing of Oligopeptide Conformations by Nearest Neighbor Interactions between Amino Acid Residues. Biomolecules, 12, 684, 2022;
  13. B. Andrews, J. Guerra, R. Schweitzer-Stenner and B. Urbanc. Do molecular dynamics force fields accurately model Ramachandran distributions of amino acid residues in water? Phys. Chem. Chem. Phys. 24, 3259-3279, 2022. https://doi: 10.1039/d1cp05069a
  14. B. Milorey, H. Schwalbe, N. O’Neill, and R. Schweitzer-Stenner. Repeating Aspartic Acid Residues Prefer Turn-like Conformations in the Unfolded State: Implications for Early Protein Folding. J. Phys. Chem. B. 125, 11392-11407, 2021.
  15. B. Milorey, R. Schweitzer-Stenner, B. Andrews, H. Schwalbe and B. Urbanc. Short peptides as predictors for the structure of polyarginine sequences in disordered proteins. Biophys.J. 120, 662-676, 2021,
  16. S. Zhang, B. Andrews, R. Schweitzer-Stenner and B. Urbanc. Intrinsic Conformational Dynamics of Alanine in Water/Ethanol Mixtures: An Experiment-Driven Molecular Dynamics Study. J. Phys. Chem. B. 124, 11600-11616, 2020.
  17. Andrews, S. Zhang, R.Schweitzer-Stenner and B. Urbanc. glycine in Water Favors the Polyproline II State. Biomolecules, 10, 1121, 2020;
  18. S. Zhang, R. Schweitzer-Stenner and B. Urbanc. Do molecular Dynamics Force Fields Capture Conformational Dynamics of alanine in Water. J. Chem. Theo. Compt. 16, 510-527, 2020,
  19. A.Kumar, S.E.Toal, D. DiGuiseppi, R. Schweitzer-Stenner and B.M. Wong. Water-Mediated Electronic Structure of Oligopeptides Probed by Their UV Circular Dichroism, Absorption Spectra, and Time Dependent DFT Calculations. J. Phys. Chem. B., 124, 2579-2590, 2020,DOI:10.1021/acs.jpcb.0c00657
  20. A. Kumar, R. Schweitzer-Stenner and B.Wong. A new interpretation of the structure and solvent dependence of the far UV circular dichroism spectrum of short oligopeptides. Chem. Comm. 55, 58701-5704, 2019. DOI: 10.1039/c9cc01513
  21. R. Schweitzer-Stenner, I. Pecht and C. Guo. Orientation of Oligopeptides in Self-assembled Monolayers Inferred from Infrared Reflection Absorption Spectroscopy, J. Phys. Chem. B., 123, 860-868, 2019; DOI: 10.1021/acs.jpcb.8b09180

  22. Protein Structure and Folding/Unfolding

  23. A. Archaryya, D. DiGuiseppi, B.L. Stinger, R. Schweitzer-Stenner, and T. D. Vaden. Structural Destabilization of Azurin by Imidazolium Chloride Ionic Liquids in Aqueous Solution. J. Phys. Chem. B. 123, 6933-6945, 2019. DOI: 101021/acs.jpcb.9b0411
  24. B. Milorey, R. Schweitzer-Stenner, R. Kurbaj and D. Malyshka. pH Induced Switch Between Different Modes of Cytochrome c Binding to Cardiolipin Containing Liposomes. ACS Omega, 4, 1386-1400, 2019;  DOI: 10.1021/acsomega.8b02574