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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 (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 (2017-2015)

Conformational Analysis and Self-Assembly of Peptides

  1. R. Schweitzer-Stenner and S.E. Toal. Anticooperative Nearest Neighbor Interactions between Residues in Unfolded Peptides and Proteins. Biophys. J. 2018, 114, 1046-1057, 2018.
  2. N.V. Ilawe, R. Schweitzer-Stenner, D. DiGuiseppi and B.M. Wong. Is a cross β-sheet structure of low molecular weight peptides necessary for the formation of fibrils and hydrogels? Phys.Chem.Chem.Phys. 2018, 20, 18158-18168.
  3. 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.
  4. 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.
  5. 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.
  6. 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.
  7. 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.
  8. 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.
  9. 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.
  10. 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.
  11. 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.
  12. 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.
  13. 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).

Cytochrome c Structure and Function

  1. R. Schweitzer-Stenner. Relating the multifunctionality of cytochrome c to membrane binding and structural conversion. Biophys. Rev, in press, DOI: 10.1007/s12551-018-0409-4, 2018.
  2. 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. 2017, 8, 1993-1998.
  3. 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. J. 2017, 23, 1151-1156.
  4. 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.
  5. 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.
  6. 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.