Reinhard Schweitzer-Stenner

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Drexel University

United States

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Reinhard Schweitzer-Stenner is a Professor at Drexel University in the United States. His research areas encompass the local and global behavior of unfolded and intrinsically disordered peptides and proteins, as well as the dynamics of conformational transitions in proteins. He has published several articles addressing topics such as peptide gelation, thermostability of gels, and the nanostructure of peptide fibrils.

Recent Grants

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Identifying the Rules Governing Tripeptide Gelation in Aqueous Solution

Open Date: 2017-08-01

Close Date: 2020-07-01

Articles (17)

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2025

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2021

Collaborators (2)

Brigita Urbanc

Professor

Drexel University

UNITED STATES

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Nicolas J. Alvarez

Drexel University

UNITED STATES

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Reinhard Schweitzer-Stenner

Research Interests

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About

Recent Grants

Articles (17)

Local and Global Behavior of Unfolded and Intrinsically Disordered Peptides and Proteins

Amber ff24EXP-GA, Based on Empirical Ramachandran Distributions of Glycine and Alanine Residues in Water

Order-to-Disorder and Disorder-to-Order Transitions of Proteins upon Binding to Phospholipid Membranes: Common Ground and Dissimilarities

Ordered Aggregates of Fmoc-Diphenylalanine at Alkaline pH as a Precursor of Fibril Formation and Peptide Gelation

Intrinsic Conformational Dynamics of Glycine and Alanine in Polarizable Molecular Dynamics Force Fields: Comparison to Spectroscopic Data

Tuning the thermostability of GHG gels by salts at different positions on the Hofmeister scale

Determining the nanostructure and main axis of gly-his-gly fibrils using the amide I’ bands in FTIR, VCD, and Raman spectra

Conformational Manifold Sampled by Two Short Linear Motif Segments Probed by Circular Dichroism, Vibrational, and Nuclear Magnetic Resonance Spectroscopy

Influence of central sidechain on self-assembly of glycine-x-glycine peptides

The relevance of short peptides for an understanding of unfolded and intrinsically disordered proteins

Heme–Protein Interactions and Functional Relevant Heme Deformations: The Cytochrome c Case

Forbidden Secondary Structures Found in Gel-Forming Fibrils of Glycylphenylalanylglycine

Exploring Nearest Neighbor Interactions and Their Influence on the Gibbs Energy Landscape of Unfolded Proteins and Peptides

Randomizing of Oligopeptide Conformations by Nearest Neighbor Interactions between Amino Acid Residues

Do molecular dynamics force fields accurately model Ramachandran distributions of amino acid residues in water?

The combined use of amide I bands in polarized Raman, IR, and vibrational dichroism spectra for the structure analysis of peptide fibrils and disordered peptides and proteins

Repeating Aspartic Acid Residues Prefer Turn-like Conformations in the Unfolded State: Implications for Early Protein Folding

Collaborators (2)

Brigita Urbanc

Nicolas J. Alvarez

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