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Professor Stenner

Reinhard Schweitzer-Stenner, PhD

Professor
Department of Chemistry
Office: Disque Hall 605a
rschweitzer-stenner@drexel.edu
Phone: 215.895.2268
Fax: 215.895.1399

Additional Sites: schweitzer-stenner.com

Education:

  • 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

  • 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 119, 13237-13251, 2015
  • 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.  51, 1698-1650, 2015
  • 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. 17, 24917-24924, 2015
  • 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, 2014
  • S.E. Toal and R. Schweitzer-Stenner. Local Order in the Unfolded State: Conformational Biases and Nearest Neighbor Interactions. Biomolecules 4, 725-773, 2014 (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. 118, 1309-1318, 2014

Cytochrome c Structure and Function

  • 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.  119, 12846-12859, 2015
  • 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. 119, 1334-1349, 2015
  • 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.  75, 86-92, 2014
  • R. Schweitzer-Stenner. Cytochrome c: A Multifunctional Protein Combining Conformational Rigidity with Flexibility. New J. Sci. http://dx.doi.org/10.1155/2014/484538, 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. 50, 3674-3676, 2014