Birgit Strodel

Germany

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Articles (21)

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Collaborators (6)

Henrike Heise

Heinrich Heine University Düsseldorf

GERMANY

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Nicklas Österlund

Stockholm University

SWEDEN

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Marc van der Kamp

Professor

University of Bristol

UNITED KINGDOM

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Vito Foderà

Københavns Universitet

DENMARK

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Carolin Huhn

Eberhard Karls Universität Tübingen

GERMANY

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Wolfgang H. Binder

Full Professor of Macromolecular Chemistry

Martin Luther University Halle-Wittenberg

GERMANY

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Birgit Strodel

Research Interests

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Articles (21)

Chameleonic Nature of Aβ: Implications for Alzheimer's and Other Amyloid Diseases

Effects of ion type and concentration on the structure and aggregation of the amyloid peptide Aβ16−22

Innovative strategies for modeling peptide–protein interactions and rational peptide drug design

Unraveling the relationship between PET surfaces and their hydrolases

Insulin amyloid morphology is encoded in H-bonds and electrostatics interactions ruling protein phase separation

Photocontrolled Reversible Amyloid Fibril Formation of Parathyroid Hormone-Derived Peptides

From Bulk to Binding: Decoding the Entry of PET into Hydrolase Binding Pockets

Influence of Wobbling Tryptophan and Mutations on PET Degradation Explored by QM/MM Free Energy Calculations

A brief history of amyloid aggregation simulations

The energy landscape of Aβ42: a funnel to disorder for the monomer becomes a folding funnel for self-assembly

Integrative modeling of guanylate binding protein dimers

A Hairpin Motif in the Amyloid-β Peptide Is Important for Formation of Disease-Related Oligomers

Transition Networks Unveil Disorder-to-Order Transformations in Aβ Caused by Glycosaminoglycans or Lipids

Discovery of All-d-Peptide Inhibitors of SARS-CoV-2 3C-like Protease

Structure and Dynamics of Human Chemokine CCL16—Implications for Biological Activity

Multiscale MD simulations of wild‐type and sickle hemoglobin aggregation

Disorder-to-order transition of the amyloid-β peptide upon lipid binding

Does the inclusion of electronic polarisability lead to a better modelling of peptide aggregation?

The Influences of Sulphation, Salt Type, and Salt Concentration on the Structural Heterogeneity of Glycosaminoglycans

Amyloid-β peptide dimers undergo a random coil to β-sheet transition in the aqueous phase but not at the neuronal membrane

Amyloid-type Protein Aggregation and Prion-like Properties of Amyloids

Collaborators (6)

Henrike Heise

Nicklas Österlund

Marc van der Kamp

Vito Foderà

Carolin Huhn

Wolfgang H. Binder

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