His primary areas of study are Raman spectroscopy, Crystallography, Polyproline helix, Stereochemistry and Dihedral angle. Raman spectroscopy is a subfield of Analytical chemistry that Reinhard Schweitzer-Stenner explores. His work deals with themes such as Spectroscopy, Peptide and Protein secondary structure, which intersect with Crystallography.
His Polyproline helix research integrates issues from Tripeptide, Circular dichroism, Ramachandran plot, Protein structure and Alanine. His Stereochemistry study incorporates themes from Raman scattering, Hapten, Binding site and Monomer. His work carried out in the field of Dihedral angle brings together such families of science as Cationic polymerization and Infrared spectroscopy.
His primary areas of investigation include Crystallography, Raman spectroscopy, Stereochemistry, Polyproline helix and Analytical chemistry. His Crystallography research incorporates elements of Spectral line, Infrared spectroscopy and Peptide. His studies examine the connections between Raman spectroscopy and genetics, as well as such issues in Molecular physics, with regards to Vibronic coupling.
His Stereochemistry research is multidisciplinary, relying on both Amino acid, Side chain, Protonation and Cardiolipin. The study incorporates disciplines such as Tripeptide, Molecular dynamics, Ramachandran plot, Protein structure and Alanine in addition to Polyproline helix. His Analytical chemistry research focuses on subjects like Dihedral angle, which are linked to Protein secondary structure.
Reinhard Schweitzer-Stenner mostly deals with Crystallography, Polyproline helix, Tripeptide, Molecular dynamics and Fibril. His Crystallography study combines topics in areas such as Spectral line and Peptide. Reinhard Schweitzer-Stenner interconnects Random coil, Ramachandran plot, Stereochemistry, Hydrogen bond and Cationic polymerization in the investigation of issues within Polyproline helix.
His Tripeptide research incorporates themes from Scientific method, Vibrational circular dichroism and Combinatorial chemistry. Reinhard Schweitzer-Stenner has included themes like Ethanol, Alanine and Chemical physics in his Molecular dynamics study. His Fibril study combines topics from a wide range of disciplines, such as Phase, Raman spectroscopy, Dipeptide, Stacking and Chirality.
His scientific interests lie mostly in Circular dichroism, Crystallography, Fibril, Solubility and Peptide. In his research on the topic of Circular dichroism, Antiparallel, Conformational ensembles, Molecular dynamics, Ramachandran plot and Alanine is strongly related with Polyproline helix. His Crystallography study frequently links to adjacent areas such as J-coupling.
His Fibril study integrates concerns from other disciplines, such as Tripeptide, Vibrational circular dichroism, Phase and Kinetics. His studies deal with areas such as Raman scattering, Oscillator strength, Fourier transform infrared spectroscopy, Polymer and Analytical chemistry as well as Solubility. His study in Peptide is interdisciplinary in nature, drawing from both Random coil, Flory–Huggins solution theory and Antiferromagnetism.
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Tripeptides adopt stable structures in water. A combined polarized visible Raman, FTIR, and VCD spectroscopy study.
Fatma Eker;Xiaolin Cao;Laurence Nafie;Reinhard Schweitzer-Stenner.
Journal of the American Chemical Society (2002)
Dihedral ψ Angle Dependence of the Amide III Vibration: A Uniquely Sensitive UV Resonance Raman Secondary Structural Probe
Sanford A. Asher;Anatoli Ianoul;Guido Mix;Mary N. Boyden.
Journal of the American Chemical Society (2001)
VIBRATIONAL ASSIGNMENTS OF TRANS-N-METHYLACETAMIDE AND SOME OF ITS DEUTERATED ISOTOPOMERS FROM BAND DECOMPOSITION OF IR, VISIBLE, AND RESONANCE RAMAN SPECTRA
X. G. Chen;Reinhard Schweitzer-Stenner;Sanford A. Asher;Noemi G. Mirkin.
The Journal of Physical Chemistry (1995)
Advances in vibrational spectroscopy as a sensitive probe of peptide and protein structure A critical review
Reinhard Schweitzer-Stenner.
Vibrational Spectroscopy (2006)
Stable conformations of tripeptides in aqueous solution studied by UV circular dichroism spectroscopy.
Fatma Eker;Kai Griebenow;Reinhard Schweitzer-Stenner.
Journal of the American Chemical Society (2003)
Possible orientational constraints determine secretory signals induced by aggregation of IgE receptors on mast cells.
E. Ortega;R. Schweitzer-Stenner;I. Pecht.
The EMBO Journal (1988)
The conformation of tetraalanine in water determined by polarized Raman, FT-IR, and VCD spectroscopy.
Reinhard Schweitzer-Stenner;Fatma Eker;Kai Griebenow;Xiaolin Cao.
Journal of the American Chemical Society (2004)
Dihedral angles of trialanine in D2O determined by combining FTIR and polarized visible Raman spectroscopy.
Reinhard Schweitzer-Stenner;Fatma Eker;Qing Huang;Kai Griebenow.
Journal of the American Chemical Society (2001)
Preferred peptide backbone conformations in the unfolded state revealed by the structure analysis of alanine-based (AXA) tripeptides in aqueous solution
Fatma Eker;Kai Griebenow;Xiaolin Cao;Laurence A. Nafie.
Proceedings of the National Academy of Sciences of the United States of America (2004)
N-Methylacetamide and Its Hydrogen-Bonded Water Molecules Are Vibrationally Coupled
X. G. Chen;Reinhard Schweitzer-Stenner;Samuel Krimm;Noemi G. Mirkin.
Journal of the American Chemical Society (1994)
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