Reinhard Schweitzer-Stenner
Department of Chemistry
Drexel University
32nd and Chestnut Streets
Philadelphia
USA
Name/email consistency: high
- Distribution of conformations sampled by the central amino acid residue in tripeptides inferred from amide I band profiles and NMR scalar coupling constants. Schweitzer-Stenner, R. J. Phys. Chem. B (2009)
- Internal electric field in cytochrome C explored by visible electronic circular dichroism spectroscopy. Schweitzer-Stenner, R. J. Phys. Chem. B (2008)
- The alanine-rich XAO peptide adopts a heterogeneous population, including turn-like and polyproline II conformations. Schweitzer-Stenner, R., Measey, T.J. Proc. Natl. Acad. Sci. U.S.A. (2007)
- Conformations of alanine-based peptides in water probed by FTIR, Raman, vibrational circular dichroism, electronic circular dichroism, and NMR spectroscopy. Schweitzer-Stenner, R., Measey, T., Kakalis, L., Jordan, F., Pizzanelli, S., Forte, C., Griebenow, K. Biochemistry (2007)
- 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. Schweitzer-Stenner, R., Gorden, J.P., Hagarman, A. J. Chem. Phys (2007)
- Conformational manifold of alpha-aminoisobutyric acid (Aib) containing alanine-based tripeptides in aqueous solution explored by vibrational spectroscopy, electronic circular dichroism spectroscopy, and molecular dynamics simulations. Schweitzer-Stenner, R., Gonzales, W., Bourne, G.T., Feng, J.A., Marshall, G.R. J. Am. Chem. Soc. (2007)
- Static normal coordinate deformations of the heme group in mutants of ferrocytochrome c from Saccharomyces cerevisiae probed by resonance Raman spectroscopy. Schweitzer-Stenner, R., Huang, Q., Hagarman, A., Laberge, M., Wallace, C.J. J. Phys. Chem. B (2007)
- Conformational substates of horse heart cytochrome c exhibit different thermal unfolding of the heme cavity. Schweitzer-Stenner, R., Shah, R., Hagarman, A., Dragomir, I. J. Phys. Chem. B (2007)
- Salmon calcitonin and amyloid beta: two peptides with amyloidogenic capacity adopt different conformational manifolds in their unfolded states. Schweitzer-Stenner, R., Measey, T., Hagarman, A., Eker, F., Griebenow, K. Biochemistry (2006)
- 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. Schweitzer-Stenner, R., Levantino, M., Cupane, A., Wallace, C., Laberge, M., Huang, Q. J. Phys. Chem. B (2006)
- The conformation of tetraalanine in water determined by polarized Raman, FT-IR, and VCD spectroscopy. Schweitzer-Stenner, R., Eker, F., Griebenow, K., Cao, X., Nafie, L.A. J. Am. Chem. Soc. (2004)
- The structure of tri-proline in water probed by polarized Raman, Fourier transform infrared, vibrational circular dichroism, and electric ultraviolet circular dichroism spectroscopy. Schweitzer-Stenner, R., Eker, F., Perez, A., Griebenow, K., Cao, X., Nafie, L.A. Biopolymers (2003)