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

Reinhard Schweitzer-Stenner, Professor Emeritus, Drexel University Department of Chemistry

Reinhard Schweitzer-Stenner, PhD

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

Additional Sites:

Google scholar


  • Venia Legendi (Habilitation), Physics, Universität Bremen, 1990
  • Dr. rer. nat. Physics, Universität Bremen, 1983
  • Diploma Physicist, Physics, Bergische Universität Wuppertal, 1980

Curriculum Vitae:

Download (PDF)

Research Interests:

  • Biophysical chemistry
  • Protein structure and function
  • Intrinsically disordered proteins
  • Structure analysis
  • Vibrational spectroscopy
  • Statistical thermodynamics


Reinhard Schweitzer-Stenner was born in Herne/Germany. He received his diploma in Physics from the University of Wuppertal (1980), his doctoral degree (Dr rer. nat.) in Physics from the University of Bremen (1983), and his habilitation (venia legendi) from this institution in 1990. After his habilitation he held a faculty position at the University of Bremen until 1999. In addition, Professor Schweitzer-Stenner worked as a visiting scientist at the Weizmann Institute in Rehovot/Israel (1985/ 1986) and the University of Michigan in Ann Arbor (1993/1994).

In 1999, he became an Associate Professor of Chemistry at the University of Puerto Rico in Rio Piedras. In 2003, he joined the faculty of the Chemistry Department at Drexel University in Philadelphia; he retired from this institution as professor emeritus in August 2022.

Schweitzer-Stenne remains active with a research group that explores the self-assembly of short peptides. Over the last 20 years, his Biospectroscopy Research Group examined the structure−function relationship of membrane-bound cytochrome c, determined conformational distributions of peptides, and explored the rules underlying the self-assembly and gelation of low molecular weight peptides. Multiple grants from the National Science Foundation supported his interdisciplinary and collaborative research. He has published more than 200 papers and book articles in peer-reviewed journals.

During his active tenure at Drexel, he taught all major physical chemistry classes at the undergraduate and graduate levels. As a result, undergraduate and graduate students from the Biospectroscopy Research Group embarked on very successful careers.

Selected Publications:

  • N. O’Neill, T.A. Lima, F.F Ferreira, N.J. Alvarez and R. Schweitzer-Stenner. Determining the Nanostructure and Main Axis of Gly-His-Gly Fibrils Using the Amide I; Bands in FTIR, VCD and Raman Spectra. Spectrochim. Acta A 306, 123584, 2024,
  • R. Schweitzer-Stenner, R. Kurbaj, N. O’Neill, B. Andrews, R. Shah, and B. Urbanc. Conformational Manifold Sampled by Two Short Linear Motif Segments Probed by Circular Dichroism, Vibrational, and Nuclear Magnetic Resonance Spectroscopy. Biochemistry, 62, 2571-2586, 2023,
  • R. Schweitzer-Stenner. The Relevance of Short Peptides for an Understanding of Unfolded and Intrinsically Disordered Proteins. Invited Perspectives article, Phys. Chem. Chem. Phys., 25, 11908–11933, 2023;
  • L. Thursch, T. Lima, N. O’Neill, F.F. Ferreira, R. Schweitzer-Stenner and N.J. Alvarez. Influence of central side chain on self-assembly of glycine-x-glycine peptides. Soft Matter, 19, 394-409, 2023;
  • R. Schweitzer-Stenner. Heme-Protein interactions and Functional Relevant Heme Deformations: The Cytochrome c Case. Molecules, 27, 8751, 2022;
  • O’Neill, T, Lima, F.F. Ferreira, L. Thursch, N. Alvarez, and R. Schweitzer-Stenner. Forbidden Secondary Structures Found in Gel-Forming Fibrils of Glycylphenylalanylglycine. J. Phys. Chem. B 126, 8080-8093, 2022;
  • R. Schweitzer. Exploring Nearest Neighbor Interactions and Their Influence on the Gibbs Energy Landscape of Unfolded Proteins and Peptides. Int. J. Mol. Sci. 23, 5643, 2022;
  • R.Schweitzer-Stenner, B. Milorey and H. Schwalbe. Randomizing of Oligopeptide Conformations by Nearest Neighbor Interactions between Amino Acid Residues. Biomolecules, 12, 684, 2022;
  • 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.
  • 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.
  • 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,
  • 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,
  • M. Hesser, L. Thursch, T.Lima, T. Lewis, N.J. Alvarez and R. Schweitzer-Stenner. Concentration Dependence of a Hydrogel Phase Formed by the Deprotonation of the Imidazole Side Chain of Glycylhistidylglycine. Langmuir, 37, 6935-6946, 2021,
  • Thursch, T. A. Lima, R. Schweitzer-Stenner and N.J. Alvarez. The impact of thermal history on the structure of glycylalanylglycine ethanol/water gels. J. Pept. Sci. 27:e.3305, 2021;
  • 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,