Most important publications from the last 2 years:
Amyloid-β peptide dimers undergo a random coil to β-sheet transition in the aqueous phase but not at the neuronal membrane
H. Fatafta, M. Khaled, M. C. Owen, A. Sayyed-Ahmad, B. Strodel Proc. Nat. Acad. Sci. USA 118, e2106210118 (2021). https://www.pnas.org/doi/10.1073/pnas.2106210118
Energy landscapes of protein aggregation and conformation switching in intrinsically disordered proteins
B. Strodel , J. Mol. Biol. 433, 167182 (2021). https://doi.org/10.1016/j.jmb.2021.167182
Disorder-to-order transition of the amyloid-β peptide upon lipid binding. H. Fatafta, B. Kav, B.F. Bundschuh, J. Loschwitz, B. Strodel
Biophys. Chem. 280, 106700 (2022). https://doi.org/10.1016/j.bpc.2021.106700
Amyloid aggregation simulations: challenges, advances and perspectives. B. Strodel. Curr. Opin. Struct. Biol. 67, 145-152 (2021). https://doi.org/10.1016/j.sbi.2020.10.019
Thermodynamics and kinetics of the amyloid-β peptide revealed by Markov state models based on MD data in agreement with experiment. A. Paul, S. Samantray, M. Anteghini, B. Strodel Chem. Sci. 12, 6652-6669 (2021). https://doi.org/10.1039/D0SC04657D
Amyloid-type Protein Aggregation and Prion-like Properties of Amyloids. D. Willbold, B. Strodel, G. F. Schröder, W. Hoyer, H. Heise. Chem. Rev. 121, 13, 8285-8307 (2021). https://pubs.acs.org/doi/full/10.1021/acs.chemrev.1c00196
Novel Inhibitors of the Main Protease of SARS-CoV-2 Identified via a Molecular Dynamics Simulation-Guided in Vitro Assay. J. Loschwitz, A. Jäckering, M. Keutmann, M. Olagunju, R. J. Eberle, M. A. Coronado, O. O. Olubiyi, B. Strodel. Bioorg. Chem. 111, 104862 (2021). https://www.sciencedirect.com/science/article/pii/S004520682100239X
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