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Reinhard Schweitzer-Stenner, Ph.D.

Department Head, Professor

Professor Stenner

Office: Disque Hall 605a
Phone: (215) 895-2268
Email: rschweitzer-stenner@drexel.edu

Fax: (215) 895-1399

Website: http://www.schweitzer-stenner.com/

Education

  • M.S.,  Physics, Bergische Universität Wuppertal (Germany), 1980
  • Dr. rer.nat, Physics, Universität Bremen (Germany), 1983

Publications

Papers which emerged from my PhD-thesis at the University of Bremen

  • R. Schweitzer-Stenner, W. Dreybrodt, A. Mayer and S. el Naggar.  Influence of the solvent environment on the polarization properties of resonance Raman scattering in hemoglobin. J . Raman  Spectrosc. 13, 139-147, 1982.
  • R. Schweitzer-Stenner, W. Dreybrodt and S el Naggar, Investigation of pH-induced Symmetry Distortions of the Prosthetic Group in Deoxyhemoglobin by Resonance Raman Scattering. Biophys. Struct. Mech. 10, 241-256, 1984.
  • S. el Naggar, R. Schweitzer-Stenner, W. Dreybrodt and A. Mayer. Determination of the Raman Tensor of the Haem Group in Myoglobin by Resonance Raman Scattering in Solution and Single Crystals.  Biophys. Struct. Mech. 10., 257-273, 1984.

University Assistant at the University of Bremen (1983-1985; 1986-1990)

  • R. Schweitzer-Stenner, W. Dreybrodt, D. Wedekind and S. el Naggar. Investigation of pH-induced symmetry distortions of the prosthetic group in oxyhaemoglobin by resonance Raman scattering. Eur. Biophys. J. 11,61-76, 1984.
  • R. Schweitzer-Stenner and W. Dreybrodt. Excitation Profiles and Depolarization Ratios of Some Prominent Raman Lines in Oxyhemoglobin and Ferrocytochrome c in the Pre-Resonant and Resonant Region of the Q-band. J. Raman Spectrosc.  16, 111-123, 1985. DOI: 10.1002/jrs.1250200311
  • S. el Naggar, W. Dreybrodt and R. Schweitzer-Stenner.  Haem-apoprotein interactions detected by resonance Raman scattering in Mb- and Hb-derivatives lacking the saltbridge His 146b-Asp 94b. Eur. Biophys. J.  12, 43-49, 1985.
  • D. Wedekind, R. Schweitzer-Stenner and W. Dreybrodt. Heme-apoprotein interaction in the modified oxyhemoglobin-bis-(N-maleimidomethyl)ether and in oxyhemoglobin at high Cl--concentration detected by resonance Raman scattering.  Biochim. Biophys. Acta.  830, 224-232, 1985.
  • D. Wedekind, U. Brunzel, R. Schweitzer-Stenner and W. Dreybrodt. Correlation of pH-dependent Resonance Raman and Optical Absorption Data Reflecting Haem-Apoprotein Interaction in Oxyhaemoglobin. J. Mol. Struc. 143, 457-460, 1986.
  • R. Schweitzer-Stenner, W. Dreybrodt, D. Wedekind and U. Kubitscheck. The Analyzation of the Depolarization Ratio Dispersion of Resonant Raman Lines in Hemeproteins. A Suitable Tool to  Detect Heme-Apoprotein Interactions. J. Mol. Struc. 143, 453-457, 1986.
  • Kubitscheck, W. Dreybrodt and R. Schweitzer-Stenner. Detection of heme distortions in ferri- and ferrocytochrome c by resonance Raman scattering. Spectrosc. Lett. 19, 681-689, 1986.  
  • U. Brunzel, W. Dreybrodt and R. Schweitzer-Stenner.  pH-dependent absorption in the B- and Q-bands of oxyhemoglobin and chemically modified oxyhemoglobin (BME) at low Cl--concentrations. Biophys. J.  49, 1069-1076, 1986.
  • R. Schweitzer-Stenner,  D. Wedekind and W. Dreybrodt. Correspondence of the pK-values of oxyHb-titration states detected by resonance Raman scattering to kinetic data of ligand dissociation  and association. Biophys. J. 49, 1077-1088, 1986.
  • U. Bobinger, R. Schweitzer-Stenner and W. Dreybrodt. Highly resolved depolarization dispersion and excitation profiles of Raman fundamentals of protoporphyrin IX in a cytochrome c matrix.  J. Raman Spectrosc.  20, 191-202, 1989.
  • R. Schweitzer-Stenner and W. Dreybrodt.  An extended MWC-model expressed in terms of the Herzfeld-Stanley  formalism applied to oxygen and carbonmonoxide binding curves of hemoglobin trout IV.  Biophys. J.  55,691-701,1989.
  • R. Schweitzer-Stenner,  D. Wedekind and W. Dreybrodt. Detection of heme perturbations caused by the quaternary R->T transition in oxyhemoglobin trout IV by resonance Raman scattering. Biophys. J. 55, 703-712, 1989.
  • R. Schweitzer-Stenner, D. Wedekind and W. Dreybrodt. The influence of structural variations in the F- and FG-helix of the b-subunit modified oxyHb-NES on the heme structure detected by resonance Raman scattering. Eur. Biophys. J.  17, 87-100, 1989.
  • E. Ortega, R. Schweitzer-Stenner  and I. Pecht. Receptor-Effector Coupling Processes Probed by Monoclonal Antibodies. In: Computer Assisted Modeling of Receptor-Ligand Interaction. Theoretical Aspects  and Applications to Drug Design. Edited by A. Golombeck and R. Rein, New York, 317-326, 1988.
  • E. Ortega, R. Schweitzer-Stenner and I. Pecht. Possible configurational constraints determine secretory signals induced by aggregation of IgE receptors on mast cells. EMBO J. 7, 4101-4109, 1988.
  • E. Ortega, R. Schweitzer-Stenner, and I. Pecht. Receptor-effector coupling processes probed by monoclonal antibodies. Prog. Clin. Biol. Res. 289, 317-326, 1989.
  • I. Pecht, R. Schweitzer-Stenner and E. Ortega. Is there specificity in Fce-receptor aggregation which leads to an effective secretory stimulus?  Prog. Immunol. 7, 676-682, 1989.

Visiting Research Scientist at the Weizmann Institute of Science, (1985-1986).

  • A.Corcia, R. Schweitzer-Stenner , I. Pecht and B. Rivnay. Characterization of the ion channel activity in planar bilayers containing IgE-Fce receptor and cromolyn binding protein.  EMBO J. 5, 849-854, 1986.
  • I. Pecht, R. Schweitzer-Stenner, R. Gertler, M. Wolf, Y. Zisman and B. Reck. Immunological stimulation of mast cells degranulation: role of cytosolic pH, Na+ and Ca2+ ions NATO ASI Series: Life Sciences, 133, 73-86.
  • R. Schweitzer-Stenner, A. Licht, I. Luescher and I. Pecht. Oligomerization and Ring Closure of Immunglobulin E Class Antibody by Divalent Haptens.  Biochemistry 26, 3602-3612, 1987.

Senior University Assistant at the University of Bremen, (1990-1994).

  • R. Schweitzer-Stenner, U. Bobinger and W. Dreybrodt.  Multimode analysis of depolarization ratio dispersion and excitation profiles of seven Raman fundamentals from the heme group in ferrocytochrome c. J. Raman Spectrosc.  22, 65-78, 1991.
  • U. Bobinger, R. Schweitzer-Stenner and W. Dreybrodt. Investigation of asymmetric perturbations of Ni(II)-octaethylporphyrin in CH2Cl2 by Raman Dispersion Spectroscopy. J. Phys. Chem.  95, 7625-7635, 1991.
  • E. Ortega, R. Schweitzer-Stenner and I. Pecht. Kinetics of ligand binding to the type I Fce receptor on mast cells. Biochemistry 30, 3473-3483, 1991.
  • U. Kubitscheck, M. Kircheis, R. Schweitzer-Stenner, W. Dreybrodt, T.M. Jovin and I. Pecht.  Fluorescence Resonance Energy Transfer on Single Living Cells: Application to Binding of Monovalent Haptens to Cell-Bound Immunoglobulin E. Biophys. J. 60, 307-318, 1991.
  • I. Pecht, E. Ortega and R. Schweitzer-Stenner. Membrane receptor clustering as a cellular stimulus - the mast cell case. In: Biological Signal Transduction.  Edited by E.M Ross and K.W.A. Wirtz, NATO ASI Series Vol. H52,  Springer Verlag, Berlin and Heidelberg, 147-161, 1991.
  • R. Schweitzer-Stenner,  A. Licht and I. Pecht. Dimerization kinetics of the IgE-class antibodies by divalent haptens. I. The Fab-hapten interactions. Biophys. J. 63, 551-562, 1992.  
  • R. Schweitzer-Stenner, A. Licht and I. Pecht. Dimerization kinetics of the IgE-class antibodies by divalent haptens. II. The interactions between intact IgE and haptens. Biophys. J. 63, 563-568, 1992.
  • R. Schweitzer-Stenner, U. Dannemann and W. Dreybrodt. Investigation of heme distortions and heme-protein coupling in isolated subunits of oxygenated hemoglobin by resonance Raman dispersion spectroscopy.  Biochemistry  31, 694-702, 1992.
  • M. Bosenbeck, R. Schweitzer-Stenner  and W. Dreybrodt. pH-induced conformational changes of the Fe2+-His F8 linkage in deoxyhemoglobin trout IV detected by the Raman active Fe2+-Ne (His F8) stretching mode. Biophys. J 61, 31-41, 1992.
  • R. Schweitzer-Stenner  and W. Dreybrodt. Investigation of Haem-Protein Coupling and Structural Heterogenity in Myoglobin and Haemoglobin by Resonance Raman Spectroscopy. J. Raman Spectrosc. 23, 539-550, 1992.  
  • R. Schweitzer-Stenner,  M. Bosenbeck and W. Dreybrodt. Raman dispersion spectroscopy probes heme distortions in deoxy-Hb trout IV involved in its T-state Bohr-effect.  Biophys. J. 64, 1194-1209, 1993.
  • A. Stichternath, R. Schweitzer-Stenner,  W. Dreybrodt, R.S. W. Mak, X.-y. Li, L. D. Sparks, J. A. Shelnutt, C.J. Medforth and K.M. Smith. Macrocycle and Substituent Vibrational Modes of Nonplanar Ni(II)-Octaethyltetraphenylporphyrin from its Resonance Raman, Near-Infrared-Excited FT-Raman, FT-IR Spectra and Deuterium Isotope Shifts.  J. Phys. Chem. 97, 3701-3708, 1993.
  • E. Unger, U. Bobinger, W. Dreybrodt and R. Schweitzer-Stenner.  Vibronic coupling in Ni(II)-porphine derived from resonant excitation profiles. J. Phys. Chem.  97, 9956-9968, 1993.  
  • H. Gilch, R. Schweitzer-Stenner and W. Dreybrodt. Structural Heterogeneity of the Fe2+-Ne(HisF8) Bond in Various Hemoglobin and Myoglobin Derivatives Probed by the Raman active Iron Histidine Stretching Mode.  Biophys. J. 65, 1470-1485, 1993.  
  • U. Kubitscheck, R. Schweitzer-Stenner,  D.J. Arndt-Jovin, T.M. Jovin and I. Pecht. Distribution of Type I Fce-Receptors on the Surface of Mast Cells Probed by Fluorescence Energy Transfer. Biophys. J.  64, 110-120, 1993.  
  • R. Schweitzer-Stenner, E. Ortega and I. Pecht. Kinetics of FceRI Dimer Formation by Specific Monoclonal Antibodies on Mast Cells. Biochemistry  33, 8813-8825, 1994.
  • R. Schweitzer-Stenner. Revisited Depolarization Ratio Dispersion of Raman Fundamentals from Heme c in Ferrocytochrome c Confirms That Asymmetric Perturbations Affect the Electronic and Vibrational Structure of the Chromophore's Macrocycle. J. Phys. Chem. 98, 9374-9379, 1994.

Research Scientist at the University of Michigan (1993-1994).

  • X.G. Chen, R. Schweitzer-Stenner, S. Krimm, N.G. Mirkin and S.A. Asher. N-Methylacetamide and Its Hydrogen-Bonded Water Molecules Are Vibrationally Coupled. J. Am. Chem. Soc. 116, 11141-11142, 1994.
  • X.G. Chen, S.A. Asher, R. Schweitzer-Stenner,  N.G. Mirkin, and S. Krimm. UV Raman Determination of the p* Excited State Geometry of N-methylacetamide: Vibrational Enhancement Pattern. J. Am. Chem. Soc. 117, 2884-2895, 1995.
  • X.G. Chen, R. Schweitzer-Stenner, S.A. Asher, N.G. Mirkin and S. Krimm. Vibrational Assignments of trans N-methylacetamide and Some of its Deuterated Isotopomers from Band Decomposition of IR, Visible and Resonance Raman Spectra. J. Phys. Chem. 99, 3074-3083, 1995. 

University Lecturer at the University of Bremen (1995-1996).

  • R. Schweitzer-Stenner, E. Unger, G. Karvounis and W. Dreybrodt. Spectral Analyses Is Suitable to Decompose Overcrowded Resonance Raman Spectra of Metallporphyrins and Yields Reliable Depolarization Ratios. J. Phys. Chem. 99, 7195-7196, 1995.
  • H. Gilch, W. Dreybrodt, and R. Schweitzer-Stenner. Thermal fluctuations between conformational substates of the Fe2+-His F8 linkage in deoxymyoglobin probed by the Raman active Fe-Ne(His F8) stretching vibration. Biophys. J., 69, 214, 1995.
  • H. Gilch, R. Schweitzer-Stenner, W. Dreybrodt, M. Leone, A. Cupane and L. Cordone. Conformational substates of the Fe2+- His F8 linkage in deoxymyoglobin and hemoglobin probed in parallel by the Raman band of the Fe-His stretching vibration and the near infrared absorption band III. Int. J. Quant.Chem. 59, 301-313, 1996.
  • W. Jentzen, E. Unger, G Karvounis, J.A. Shelnutt, W. Dreybrodt, and R. Schweitzer-Stenner. Conformational Properties of Nickel(II) Octaethyl-porphyrin in Solution. I. Resonance Excitation Profiles and Temperature Dependence of Structure Sensitive Raman Lines. J. Phys. Chem., 100, 14184-14191, 1996.  
  • A. Cupane, M. Leone, L. Cordone, H. Gilch, W. Dreybrodt, E. Unger and R. Schweitzer-Stenner. Conformational Properties of Nickel(II)-Octaethylporphyrin in Solution. II. A Low Temperature Optical Absorption Spectroscopy Study. J. Phys. Chem., 100, 14192-14199, 1996.
  • I. Tamir, R. Schweitzer-Stenner and I. Pecht. Immobilization of the type I receptor for IgE initiates signal transduction in mast cells. Biochemistry, 35, 6872-6883, 1996.  

Distinguished Professor at the University of Bremen (1996-1999).

  • R. Schweitzer-Stenner, A. Stichternath, W. Dreybrodt, W. Jentzen, X.-Z. Song, J.A. Shelnutt, O.F. Nielsen, C.J. Medforth and K.M. Smith.  Raman Dispersion Spectroscopy on the Highly Saddled Nickel(II)-Octaethyltetraphenylporphyrin Reveals the Symmetry of Non-Planar Distortions and the Vibronic Coupling Strength of Normal Modes.  J. Chem. Phys. 107,1794-1815, 1997.  
  • E. Unger, W. Dreybrodt, and R. Schweitzer-Stenner. Conformational Properties of Nickel(II)-meso-Tetraphenylporphyrin in Solution. Raman Dispersion Spectroscopy Reveals the Symmetry of Distortions for a Nonplanar Conformer. J. Phys. Chem. A, 101, 5997-6007, 1997.  
  • W. Jentzen, E. Unger, X-Z. Song, I. Turowska-Tyrk, R. Schweitzer-Stenner, W. Dreybrodt, R.W. Scheidt, and J.A. Shelnutt. Planar and Nonplanar Conformations of (Meso-Tetraphenyl-porphinato)nickel(II) in Solution as Inferred from Solution and Solid-State Raman Spectroscopy.  J. Phys. Chem. A, 101, 5789-5798, 1997.  
  • G. Sieler and R. Schweitzer-Stenner. The Amide I Mode of Peptides in Aqueous Solution Involves Vibrational Coupling Between The Peptide Group and Water Molecules of The Hydration Shell. J. Am. Chem. Soc. 119, 1720-1726, 1997.
  • S. A. Asher, P. Li, Z. Chi, X.G. Chen, R. Schweitzer-Stenner, N.G. Mirkin, and S. Krimm. Reply to:”Comment on ‘Vibrational Assignments of trans-N-Methylacetamide and Some of Its Deuterated Isotopomers from Band Decomposition of IR, Visible, and Resonance Raman Spectra’. J. Phys. Chem. A  101, 3992-3994, 1997.  
  • R. Schweitzer-Stenner,  I. Tamir and I. Pecht. Analysis of Fc?RI-Mediated Mast Cell Stimulation by Surface-Carried Antigens. Biophys. J., 72, 2470-2478, 1997.  
  • U. Lippert, M. Artuc, A. Grützkau, A. Möller, A Kenderessy-Szabo, D. Schadendorf, J. Norgauer, K. Hartmann, R. Schweitzer-Stenner, B.M. Henz, and S. Krüger-Krtasagakes.  Expression and Functional Activity of the IL-8 Receptor Type CXCR1 and CXCR2 on Human Mast Cells. J. Immunol. 161, 2600-2608, 1998.  
  • R. Schweitzer-Stenner, G. Sieler, N.G. Mirkin and S. Krimm.  Intermolecular Coupling in Liquid and Crystalline States of trans N-Methylacetamide Investigated by Polarized Raman and FT-IR  Spectroscopies.  J. Phys. Chem. A. 102, 118-127, 1998.
  • A. Cupane, M. Leone, E. Unger, C. Lemke, M. Beck, W. Dreybrodt, and R. Schweitzer-Stenner.  Dynamics of various metal-octaethylporphyrins in solution studied through resoance Raman and low-temperature optical absorption spectroscopies.  Role of the central metal. J. Phys. Chem. B, 102, 6612-6620,1998.
  • C. Lemke, W. Dreybrodt, J.A. Shelnutt, J.M.E. Quirke and R. Schweitzer-Stenner. Polarized Raman Dispersion Spectroscopy probes planar and non-planar distortions ofNi(II)-porphyrins with different peripheral substituents. J. Raman Spectrosc., 29, 945-953, 1998 (Invited paper, guest editor: W. Kiefer, special issue on Resonance Raman Spectroscopy).
  • R. Schweitzer-Stenner, G. Sieler H. Christiansen. Competition between peptide-peptide and peptide-solvent hydrrogen bonding probed by polarized Raman spectroscopy on N’-methylacetamide. Asian J. Phys. 7, 287-312, 1998 (Invited paper, guest editor: W. Kiefer, special issue on the 70th anniversary of the discovery of the Raman effect).
  • E. Unger, R.J. Lipski, W. Dreybrodt and R. Schweitzer-Stenner. A New Method for the Evaluation of Normal Modes and Molecular Mechanics with Reduced Sets of Force Constants. 1. Principle and Reliability Test. J. Raman Spectrosc. 30, 3-28, 1999. DOI: 10.1002/(SICI)1097-4555(199901)30:1<3::AID-JRS340>3.0.CO;2-3
  • G. Sieler, R. Schweitzer-Stenner, J.S.W. Holtz, V. Pajcini and S.A. Asher.  Different Conformers and Protonation States of Dipeptides Probed by Polarized Raman, UV-resonance Raman and FTIR-spectroscopy.  J. Phys. Chem. B. 103, 372-384, 1999. DOI: 10.1021/jp9825462 
  • R.J. Lipski, E. Unger, and R. Schweitzer-Stenner. Polarized Resonance Raman Spectroscopy Reveals Two Different Conformers of Metallo(II)octamethylchlorins in CS2. J. Phys. Chem. B., 103, 9777-9781, 1999. DOI: 10.1021/jp9918858.
  • E. Unger, M. Beck, R.J. Lipski, W. Dreybrodt, C.J. Medforth, K.M. Smith, and R. Schweitzer-Stenner.  A New Method for Evaluating the Conformations and Normal Modes of Macromolecule Vibrations.  2. Application to nonplanarily distorted metal porphyrins.  J. Phys. Chem. B., 103, 10022-10031, 1999. DOI: 10.1021/jp992045w. 
  • R. Schweitzer-Stenner, Michael Engelke, Arieh Licht and Israel Pecht.  Mast cell stimulation by co-clustering the type I Fce-receptors with mast cell function-associated antigens. Immunol. Lett. 68, 71-78, 1999.  DOI: 10.1016/S0165-2478(99)00032-2.
  • N. Engler, A. Ostermann, A. Grassmann, D.C. Lamb, V.E. Prusakov, J. Schott, R. Schweitzer-Stenner, and F.G. Parak.  Protein dynamics in an intermediate state of myoglobin: Investigations by optical absorption spectroscopy, resonance Raman spectroscopy and X-ray structure analysis. Biophys. J., 78, 2081-2092, 2000. DOI: 0006-3495/00/04/2081/12.

Papers submitted after assuming an Associated Professorship at the University of Puerto Rico (1999-2003).

  • R. Schweitzer-Stenner, A. Cupane, M. Leone, C. Lemke, J. Schott, and W. Dreybrodt. Anharmonic protein motions and heme deformations in myoglobin cyanide probed by absorption and resonance Raman spectroscopy. J. Phys. Chem. B. 19, 4754-4764, 2000. DOI: 10.1021/jp991599w.
  • G. Mix, R. Schweitzer-Stenner, and S.A. Asher.  Uncoupled Adjacent Amide Vibrations in Small Peptides. J. Am. Chem. Soc. 122, 9028-9029, 2000.  DOI: 10.1021/ja0004783
  • R.J. Lipski, E. Unger, W. Dreybrodt, V. Militello, M. Leone, and R. Schweitzer-Stenner. Vibrational Analysis of Ni(II)- and Cu(II)-Octamethylchlorin by Polarized Resonance Raman and FTIR Spectroscopy.  J. Raman Spectrosc. 32, 521-542, 2001 (Invited paper, guest editor: H. Schrötter, special issue dedicated to celebrate the 90th birthday of Prof. Shorygin). DOI: 10.1002/jrs.728
  • C. Lemke, R. Schweitzer-Stenner, J.A. Shelnutt, and J.M. Quirke. Vibrational Analysis if Metalloporphyrins with Electron Withdrawing NO2 – Substitutents at Different meso Positions. J. Phys. Chem. A, 105, 6668-6679, 2001. DOI: 10.1021/jp011137u.
  • R. Schweitzer-Stenner, C. Lemke, R. Haddad, Y. Qiu, J.A. Shelnutt, J.M. Quirke, and W. Dreybrodt. Conformational Distortions of Metalloporphyrins With Electron Withdrawing NO2 Substituents at Different meso Positions. A Structural Analysis By Polarized Resonance Raman Dispersion Spectroscopy and Molecular Mechanics Calculations.  J. Phys. Chem. A., 105, 6680-6694, 2001. DOI: 10.1021/jp010936+.
  • M. Heid, S. Schlücker, U. Schmitt, T. Chen, R. Schweitzer-Stenner, V. Engel and W. Kiefer. Two-dimensional probing of ground state vibrational dynamics in porphyrin molecules by fs-CARS. J. Raman Spectrosc. 32, 771-784, 2001. DOI: 10.1002/jrs.741.
  • J. Schott, W. Dreybrodt, and R. Schweitzer-Stenner. The Fe2+-HisF8 Raman Band Shape of Deoxymyoglobin Reveals Taxonomic Conformational Substates of the Proximal Linkage.  Biophys. J., 81,1624-1631, 2001. DOI: 0006-3495/01/09/1624/08. 
  • R. Schweitzer-Stenner and D. Bigman. Electronic and Vibronic Contributions to The Band Splitting in Optical Spectra of Heme Proteins. J. Phys. Chem. B. 105, 7064-7073, 2001. DOI: 10.1021/jp010703i.
  • R. Schweitzer-Stenner, F. Eker, Q. Huang, and K. Griebenow. The Dihedral Angles of Tri-Alanine in D2O Determined by Combining FTIR- and Polarized Visible Raman Spectroscopy. J. Am. Chem. Soc., 123, 9628-9633, 2001. DOI: 10.1021/ja016202s.
  • S.A. Asher, A. Ianoul, G. Mix, M.N. Boden, A. Karnoup, M. Diem, and R. Schweitzer-Stenner.  Dihedral y Angle Dependence of the Amide III Vibration: A Uniquely Sensitive UV Resonance Raman Secondary Structural Probe. J. Am. Chem. Soc., 123, 9628-9633, 2001. DOI: 10.1021/ja0039738.
  • R. Schweitzer-Stenner. Dihedral angles of Tripeptides in Solution Determined by Polarized Raman and FTIR Spectroscopy. Biophys. J. 83, 523-532, 2002.  DOI: 0006-3495/02/07/523/10.
  • R. Schweitzer-Stenner, F. Eker, Q. Huang, K. Griebenow, P. Mrosz, and P.M. Kozlowski. Structure Analysis of Dipeptides in Water By Exploring and Utilizing the Structural Sensitivity of Amide III by Polarized Visible Raman, FTIR-Spectroscopy and DFT based normal coordinate analysis.  J. Phys. Chem. B. 106,4294-4304, 2002.  DOI: 10.1021/jp0137118.
  • W. Al-Azzam, E.A. Pastrana, Y.Ferrer, Q.Huang, R.Schweitzer-Stenner, and Kai Griebenow. Structure of PEG-modified HRP in organic solvents.  IR amide I spectral changes upon protein dehydration are largely due to protein structural changes and not to water removal per se. Biophys. J., 83, 363-3651, 2002.  DOI: 0006-3495/02/12/3637/15.
  • F. Eker, X. Cao, L. Nafie, and R. Schweitzer-Stenner. Tripeptides Adopt Stable Structures in Water. A Combined Polarized Visible Raman, FTIR and VCD Spectroscopy Study. J. Am. Chem. Soc. 124, 14330-14341, 2002. DOI: 10.1021/ja027381w.
  • F. Eker, X. Cao, L. Nafie, and R. Schweitzer-Stenner. The Structure of Alanine Based Tripeptides in Water and Dimethylsulfoxide Probed by Vibrational Spectroscopy. J. Phys. Chem. B., 107, 358-365, 2003. DOI: 10.1021/jp026958t.
  • M. Laberge, Q. Huang, R. Schweitzer-Stenner, and J. Fidy. The Endogenous Calcium Ions of Horseradish Peroxidase C are Required to Maintain the Functional Nonplanarity of the Heme. Biophys. J., 84, 2542-2552, 2003. DOI: 0006-3495/03/04/2542/11.
  • Q. Huang, W. Al-Azzam, K. Griebenow, and Reinhard Schweitzer-Stenner. Heme Structural Perturbation of PEG-Modified Horseradish Peroxidase C in Aromatic Organic Solvents Probed by Optical Absorption and Resonance Raman Dispersion Spectroscopy.  Biophys. J., 84, 3285-3298, 2003. DOI: 0006-3495/03/05/3285/14.
  • Q. Huang, K. Szigeti, J. Fidy and R. Schweitzer-Stenner. Structural Disorder of Native Horseradish Peroxidase C probed by Resonance Raman and Low Temperature Optical Absorption spectroscopy. J. Phys. Chem. B, 107, 2822-2830, 2003. DOI: 10.1021/jp026935e.
  • Q. Huang, M. Laberge, K. Szigeti, J. Fidy, and R. Schweitzer-Stenner. Change of The Iron Spin State in Horseradish Peroxidase C Induced By the Removal of Ca2+ probed by Resonance Raman Spectroscopy. Biopolymers (Biospectroscopy), 72, 241-248, 2003. DOI: 10.1002/bip.10417. 
  • F. Eker, K. Griebenow, and R. Schweitzer-Stenner. Stable Conformations of Tripeptides in Aqueous Solution Studied by UV Circular Dichroism Spectroscopy. J. Am. Chem. Soc. 125, 8178-8185, 2003. DOI: 10.1021/ja034625j.
  • W. Dreybrodt, J. Schott, and R. Schweitzer-Stenner. Comments to the paper "Temperature dependence of the iron-histidine Resonance Raman Band of deoxyheme proteins: Anharmonic coupling versus distribution over taxonomic conformational substates&ldquo; by Korostishevsky et al. Biophys. J., 86, 660-661, 2004. DOI: 86/1/660/02.

Papers submitted after assuming an Associate Professorship at Drexel University (2003-2008).

  • R. Schweitzer-Stenner, F. Eker, A. Perez, K. Griebenow, X. Cao, and L. Nafie. The Structure of Tri-Proline in Water Probed by Polarized Raman, FTIR, VCD and ECD Spectroscopy. Biopolymers (Peptide Science), 71, 558-568, 2003. DOI: 10.1002/bip.10534.
  • R. Schweitzer-Stenner, F. Eker, K. Griebenow, X. Cao, and L. Nafie. The Conformation of Tetraalanine in Water Determined by Polarized Raman, FTIR and VCD ". J. Am. Chem. Soc. 126, 2768-2776, 2004. DOI: 10.1021/ja039452c, Correction DOI: 10.1021/ja045638f.
  • F. Eker, K. Griebenow, X. Cao, L. Nafie, and R. Schweitzer-Stenner. Tripeptides with Ionizable Side-Chains Adopt a Perturbed Polyproline II Structure in Water. Biochemistry, 43, 613-621, 2004. DOI: 10.1021/bi035740+.
  • Q. Huang and R. Schweitzer-Stenner. Conformational analysis of tetrapeptides by exploiting the excitonic coupling between amide I modes. J. Raman Spectros. 35, 586, 2004. DOI: 10.1002/jrs.1201. 
  • F. Eker , K. Griebenow, X. Cao, L.A. Nafie and R. Schweitzer-Stenner. Preferred peptide backbone conformations in the unfolded state revealed by the structure analysis of alanine-based (AXA) tripeptides in aqueous solution. Proc. Natl. Acad. Sci. USA 101 (27), 11054, 2004. DOI: 10.1073/pnas.0402623101. Correction DOI: 10.1073/pnas.0404696101.
  • R. Schweitzer-Stenner. Secondary Structure Analysis of Polypeptides Based on an Excitonic Coupling Model to Describe the Band Profile of Amide I&rsquo; of IR, Raman and Vibrational Circular Dichroism Spectra. J. Phys. Chem B. 108, 16965, 2004. DOI: 10.1021/jp0477654.
  • F. Eker , K. Griebenow and R. Schweitzer-Stenner. AB1-28 Fragment of the Amyloid Peptide Predominantly Adopts a Polyproline II Conformation in Acidic Solution. Biochemistry, 43, 6893-6898, 2004. DOI: 10.1021/bi049542+.
  • Q. Huang, Q. Huang, R. Pinto, K. Griebenow, R. Schweitzer-Stenner, and W.J. Weber. Inactivation of Horseradish Peroxidase by Phenoxyl Radical Attack. J. Am. Chem. Soc., 127, 1431-1437, 2005. DOI: 10.1021/ja045986h.
  • Q. Huang and R. Schweitzer-Stenner. Nonplanar Heme Deformations and Excited State Displacements in Horseradish Peroxidase Detected by Raman Spectroscopy at Soret Excitation. J. Raman Spectrosc. (special issue on &lsquo;Structure and Dynamics of Biomolecules) 36 (4), 363-375, 2005. DOI: 10.1002/jrs.1326.
  • R. Schweitzer-Stenner. Structure and Dynamics of Biomolecules probed by Raman Spectroscopy. J. Raman Spectrosc. 36 (4), 276-275, 2005. DOI: 10.1002/jrs.1321.
  • R. Schweitzer-Stenner and I. Pecht. Death of a Dogma or Enforcing the Artificial? Monomeric IgE binding may initiate mast cells response by inducing its receptor aggregation. J. Immunol. (cutting edge article), 174, 4461-4464, 2005. DOI: 0022-1767/05.
  • A. Licht, I. Pecht and R. Schweitzer-Stenner. Regulation of mast cells&rsquo; secretory response by co-clustering the Type 1 Fce receptor with the mast cell function-associated antigen. Eur. J. Immunol., 35 (5), 1621-1633, 2005. DOI: 10.1002/eji.200425964.
  • T. Measey, A. Hagarman, F. Eker, K. Griebenow and R. Schweitzer-Stenner. Side chain dependence of intensity and wavenumber position of amide I&rsquo; in IR and visible Raman spectra of XA and AX dipeptides. J. Phys. Chem. B. 109, 8195-8205, 2005. DOI: 10.1021/jp045762l.
  • T. Measey and R. Schweitzer-Stenner. Simulation of amide I band profiles of trans-polyproline based on an excitonic coupling model. Chem. Phys. Letts. 408, 123-127, 2005. DOI: 10.1016/j.cplett.2005.04.014.
  • M. Levantino, Q. Huang, A. Cupane, M. Laberge, A. Hagarman and R. Schweitzer-Stenner. The importance of vibronic perturbations in ferrocytochrome c spectra: A reevaluation of spectral properties based on low-temperature optical absorption, resonance Raman, and molecular-dynamics simulations. J. Chem. Phys. 123, 054508, 2005. DOI: 10.1063/1.1961556.
  • Q. Huang, C. J. Medforth, and R. Schweitzer-Stenner*. Nonplanar Heme deformations and Excited State Displacements in Nickel Porphyrins Detected by Raman Spectroscopy at Soret Excitation. J. Phys. Chem. A. 109, 14093-10502, 2005. DOI: 10.1021/jp052986a.
  • T. Measey, and R. Schweitzer-Stenner. The Conformations Adopted by The Octamer Peptide (AAKA)2 in Aqueous Solution Probed By FTIR and Polarized Raman Spectroscopy. J. Raman Spectrosc. (invited article for a special issue celebrating the 65th birthday of Prof. Wolfgang Kiefer), 37, 248-254, 2006. DOI: 10.1002/jrs.1455.
  • A. Hagarman, T. Measey, R. Doddasomayajula, I. Dragomir, F. Eker, K. Griebenow, and R. Schweitzer-Stenner.  Conformational Analysis of XA and AX Dipeptides in Water by Electronic Circular Dichroism and 1H NMR Spectroscopy.  J. Phys. Chem.  B.  (2006) 110, 6979-6986. DOI: 10.1021/jp0561625.
  • R. Schweitzer-Stenner, T. Measey, A. Hagarman, F. Eker, and K. Griebenow.  Salmon Calcitonin and Amyloid b:  Two Peptides with Amyloidogenic Capacity Adopt Different Conformational Manifolds in Their Unfolded States.  Biochemistry. (2006) 45, 2810-2819. DOI: 10.1021/bi052282r.
  • I.C. Dragomir, T.J. Measey, A.M. Hagarman, and R. Schweitzer-Stenner.  Environment-Controlled Interchromophore Charge Transfer Transitions in Dipeptides Probed by UV Absorption and Electronic Circular Dichroism Spectroscopy.  J. Phys. Chem. B.  (2006) 110, 13235-13241. DOI: 10.1021/jp0616260.
  • T. J. Measey, and R. Schweitzer-Stenner.  Aggregation of the Amphipathic Peptides (AAKA)n into Antiparellel b-Sheets.  J. Am. Chem. Soc.  (2006) 128, 13324-13325. DOI: 10.1021/ja0632411.
  • R. Schweitzer-Stenner, M. Levantino, A. Cupane, C. Wallace, M. Laberge, and Q. Huang.  Functionally Relevant Electric Field Induced Perturbations of the Prosthetic Group of Yeast Ferrocytochrome c Mutants Obtained From a Vibronic Analysis of Low Temperature Absorption Spectra.  (2006) J. Phys. Chem. B. 110, 12155-12161. DOI: 10.1021/jp060755d.
  • R. Schweitzer-Stenner, T. Measey, L. Kakalis, F. Jordan, S. Pizzanelli, C. Forte, and K. Griebenow.  Conformations of Alanine-Based Peptides in Water Probed by FTIR, Raman, Vibrational Circular Dichroism, Electronic Circular Dichroism, and NMR Spectroscopy.  Biochemistry (2007)  46 (6), 1587-1596. DOI: 10.1021/bi062224l.
  • I. Dragomir, A. Hagarman, C. Wallace, and R. Schweitzer-Stenner.  Optical Band Splitting and Electronic Perturbations of the Heme Chromophore in Cytochrome c at Room Temperature Probed by Visible Electronic Circular Dichroism Spectroscopy.  (2007)  Biophys. J. 92, 989-998. DOI: 10.1529/biophysj.106.095976. 
  • R. Schweitzer-Stenner and T. Measey.  The Alanine-Rich XAO Peptide Adopts a Heterogeneous Population, Including Turn-Like and PPII Conformations. (2007)  Proc. Natl. Acad. Sci. 104, 6649-6654. DOI: 10.1073/pnas.0700006104.
  • R. Schweitzer-Stenner, Q. Huang, A. Hagarman, M. Laberge, and C. Wallace. Static normal coordinate deformations of the heme group in mutants of ferro-cytochrome c from Saccharomyces Cerevisiae probed by resonance Raman spectroscopy.  (2007) J. Phys. Chem. B., 111, 6527-6533. DOI: 10.1021/jp070445a.
  • R. Schweitzer-Stenner, R. Shah, A. Hagarman, and I. Dragomir.  Conformational Substates of Horse Heart Cytochrome c Exhibit Different Thermal Unfolding of the Heme Cavity.  (2007) J. Phys. Chem. B. 111, 9603-9607. DOI: 10.1021/jp069022j.
  • R. Schweitzer-Stenner, J. P. Gordon, A. Hagarman.  The Asymmetric Band Profile of the Soret Band of Deoxymyoglobin is Caused by Electronic and Vibronic Perturbations of the Heme Group Rather Than by a Doming Deformation.  (2007)  J. Chem. Phys.  127, 135103, 2007. DOI: 10.1063/1.2775931.
  • R. Schweitzer-Stenner, W. Gonzales, G. T. Bourne, J.A. Feng, and G.R. Marshall. The Conformational Manifold of -Aminoisobutyric Acid (Aib) Containing Alanine-Based Tripeptides in Aqueous Solution Explored by Vibrational Spectroscopy, Electronic Circular Dichroism Spectroscopy, and Molecular Dynamics Simulations. J. Am. Chem. Soc. 129, 13095-13109, 2007. DOI: 10.1021/ja0738430.
  • S. Pizzanelli, C. Forte,S. Monti and R. Schweitzer-Stenner. Interaction of a Tripeptide with Cesium Perfluorooctanoate Micelles. J. Phys. Chem. B. 112, 1251-1261, 2008. DOI: 10.1021/jp073947x.
  • N. Hadjiliadis, K. Panagiotou, M. Panagopoulou, T. Karavelas, V. Dokorou, A. Hagarman, J. Soffer, R. Schweitzer-Stenner and G. Malandrinos. Cu(II) and Ni(II) interactions with the terminally blocked hexapeptide Ac-Leu-Ala-His-Tyr-Asn-Lys-amide, (LAHYNK) model of histone H2B (80-85). Bioinorganic Chem.  Appl., 2008, 257038, 2008. DOI: 10.1155/2008/257038.  
  • R. Shah and R. Schweitzer-Stenner. Structural changes of horse heart ferricytochrome c induced by changes of ionic strength and anion binding. Biochemistry, 47, 5250-5257 , 2008. DOI: 10.1021/bi702492n.
  • R. Schweitzer-Stenner. The Internal Electric Field in Cytochrome C Explored by Visible Electronic Circular Dichroism Spectroscopy. J. Phys. Chem. B. 112(33); 10358-10366, 2008. DOI: 10.1021/jp802495q.
  • A. Hagarman, C. Wallace, M. Laberge, and R. Schweitzer-Stenner. Out-of-plane deformations of the heme group in different ferrocytochrome c proteins probed by resonance Raman spectroscopy. J. Raman Spectrosc., 9999, 2008. DOI: 10.1002/jrs.2050.
  • A. Hagarman, Duitch, Laura, and Schweitzer-Stenner, Reinhard. The Conformational Manifold of Ferricytochrome c Explored by Visible and Far-UV Electronic Circular Dichroism. Biochemistry, 47(36); 9667-9677, 2008.  DOI: 10.1021/bi800729w.
  • D. Verbaro, Hagarman, Andrew, Soffer, Jonathan Soffer, and Schweitzer-Stenner, Reinhard. The pH Dependence of the 695 nm Charge Transfer Band Reveals the Population of an Intermediate State of the Alkaline Transition of Ferricytochrome c at Low Ion Concentrations. Biochemistry, 48 (13) 2990-2996, 2009. DOI: 10.1021/bi802208f.
  • D. Verbaro, A. Hagarman, A. Kohli and R.Schweitzer-Stenner. Microperoxidase 11: a model system for porphyrin networks and heme–protein interactions. J. Bio. Inorg. Chem., in press, 2009. DOI: 10.1007/s00775-009-0574-9.
  • S. Yang, J-M. Yuan, J. Shin, T.j. Measey, and R. Schweitzer-Stenner and F-Y Li. Energy Landscape Associated with the Self-Aggregation of an alanine-Based Oligopeptide (AAKA). J. Phys. Chem. B. 113, 6054-6061, 2009. DOI: 10.1021/jp809279r.
  • R. Schweitzer-Stenner. Distributions of Conformations Sampled by The Central Amino Acid in Tripeptides Inferred from amide I Band Profiles and Scalar NMR Coupling Constants, J. Phys. Chem. B. 113, 2922-2932, 2009. DOI: 10.1021/jp8087644.
  • A. Hagarman, T. Measey, D. Mathieu, H. Schwalbe and R. Schweitzer-Stenner. Intrinsic Propensities of Amino Acid Residues in GxG Peptides Inferred from Amide I′ Band Profiles and NMR Scalar Coupling Constants. J. Am. Chem. Soc., ASAP, 2009. DOI: 10.1021/ja9058052.
  • T.J. Measey, K. Smith, S. Decatur, L. Zhao, G. Yang and R. Schweitzer-Stenner. The Self-aggregation of A Polyalanine Octamer Promoted by Its C-Terminal Tyrosine And Probed By A Strongly Enhanced VCD Signal. J. Am. Chem. Soc. (communication), 131 (51) 18218-18219, 2009. DOI: 10.1021/ja908324m.
  • L. Tooke, L. Duitch, T.J. Measey and R. Schweitzer-Stenner. Kinetics of the Self-Aggregation and Film Formation of Poly-L-Proline at High Temperatures Explored by Circular Dichroism Spectroscopy. Biopolymers, in press, 2010. DOI: 10.1002/bip.21361
  • T.J. Measey, K. Smith, S. Decatur, L. Zhao, G. Yang and R. Schweitzer-Stenner. The Self-aggregation of A Polyalanine Octamer Promoted by Its C-Terminal Tyrosine And Probed By A Strongly Enhanced VCD Signal. J. Am. Chem. Soc. (communication), 131, 18218-18219, 2009. 
  • L. Tooke, L. Duitch, T.J. Measey and R. Schweitzer-Stenner. Kinetics of the Self-Aggregation and Film Formation of Poly-L-Proline at High Temperatures Explored by Circular Dichroism Spectroscopy. Biopolymers, in press, 2010.
  • A. Hagarman, T.J. Measey, D. Mathieu, H. Schwalbe and R. Schweitzer-Stenner. Intrinsic Propensities of Amino Acid Residues in GXG peptides Inferred from Amide I&rsquo; Band Profiles and NMR Scalar Coupling Constants. J. Am. Chem. Soc.132, 540-551, 2010.
  • S. Pizzanelli, C. Forte, S. Monti, G. Zandomeneghi, A. Hagarman, T.J. Measey, and Reinhard Schweitzer-Stenner. J. Phys. Chem. C., in press, 2010.
  • T. J. Measey and R. Schweitzer-Stenner, Simulation of IR, Raman and VCD Amide I Band Profiles of Self-Assembled Peptides. Spectroscopy, in press, 2010.

Invited review articles (1989 - Present).

  • R. Schweitzer-Stenner. Allosteric linkage indiced distortions of the prosthetic group in heme proteins as derived from the theoretical interpretation of the depolarization ratio in resonance Raman scattering. Q. Rev. Biophys. 32, 381-490, 1989.
  • R. Schweitzer-Stenner. Parameters determining the stimulatory capacity of the type I Fce-receptor. Immunol. Lett. 68, 59-69, 1999. DOI: 10.1016/S0165-2478(99)00031-0. 
  • R. Schweitzer-Stenner. Polarized Resonance Raman Dispersion Spectroscopy on Metalporphyrins. J. Porphyr. Phthal. 5, 198-224, 2001.
  • R. Schweitzer-Stenner. Visible and UV-resonance Raman spectroscopy on model peptides. J. Raman Spectrosc., 32,711-732, 2001. DOI: 10.1002/jrs.757.
  • R. Schweitzer-Stenner. Advances in Vibrational Spectroscopy as a Sensitive Probe of Peptide and Protein Structure. A critical review.  Vib. Spectrosc. 98-117, 2006. DOI: 10.1016/j.vibspec.2006.01.004
  • R. Schweitzer-Stenner. Conformational analysis of unfolded peptides by vibrational spectroscopy. In: Unfolded Proteins. From Denatured States to Intrinsically Disordered, Ed. T. Creamer. Novalis Pres, 101-142, 2008.
  • R. Schweitzer-Stenner, T. Measey, A. Hagarman, and I. Dragomir. The Structure of unfolded peptides and proteins explored by Raman and IR spectroscopies. In: Assessing Structures and Conformation of Intrinsically Disordered Proteins”, Editors: S. Longhi and V.N. Uversky. Wiley & Sons, in press, 2008.
  • R. Schweitzer-Stenner, A. Hagarman, D. Verbaro and J. Soffer.  Conformational Stability of Cytochrome c Probed by Optical Spectroscopy, Meth. Enzymol.109-153, 2009. DOI: 10.1016/S0076-6879(09)66006-7