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Shared metadata for data-centric materials science.
- Published in:
- Scientific Data, 2023, v. 10, n. 1, p. 1, doi. 10.1038/s41597-023-02501-8
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Shared metadata for data-centric materials science.
- Published in:
- Scientific Data, 2023, v. 10, n. 1, p. 1, doi. 10.1038/s41597-023-02501-8
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- Publication type:
- Article
Crystal Structure and NMR of an α,δ‐Peptide Foldamer Helix Shows Side‐Chains are Well Placed for Bifunctional Catalysis: Application as a Minimalist Aldolase Mimic.
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- Angewandte Chemie, 2023, v. 135, n. 36, p. 1, doi. 10.1002/ange.202305326
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Titelbild: Crystal Structure and NMR of an α,δ‐Peptide Foldamer Helix Shows Side‐Chains are Well Placed for Bifunctional Catalysis: Application as a Minimalist Aldolase Mimic (Angew. Chem. 36/2023).
- Published in:
- Angewandte Chemie, 2023, v. 135, n. 36, p. 1, doi. 10.1002/ange.202309523
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Crystal Structure and NMR of an α,δ‐Peptide Foldamer Helix Shows Side‐Chains are Well Placed for Bifunctional Catalysis: Application as a Minimalist Aldolase Mimic**.
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- Angewandte Chemie International Edition, 2023, v. 62, n. 36, p. 1, doi. 10.1002/anie.202305326
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- Article
Cover Picture: Crystal Structure and NMR of an α,δ‐Peptide Foldamer Helix Shows Side‐Chains are Well Placed for Bifunctional Catalysis: Application as a Minimalist Aldolase Mimic (Angew. Chem. Int. Ed. 36/2023).
- Published in:
- Angewandte Chemie International Edition, 2023, v. 62, n. 36, p. 1, doi. 10.1002/anie.202309523
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- Article
Better force fields start with better data: A data set of cation dipeptide interactions.
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- Scientific Data, 2022, v. 9, n. 1, p. 1, doi. 10.1038/s41597-022-01297-3
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- Article
Cover Image, Volume 121, Issue 3.
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- International Journal of Quantum Chemistry, 2021, v. 121, n. 3, p. 1, doi. 10.1002/qua.26284
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The conformational space of a flexible amino acid at metallic surfaces.
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- International Journal of Quantum Chemistry, 2021, v. 121, n. 3, p. 1, doi. 10.1002/qua.26369
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- Article
Struktur und Reaktivität der Al‐O(H)‐Al‐Einheiten in Siloxidgerüstverbindungen – Modellstudien in Lösung und in Isolation.
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- Angewandte Chemie, 2019, v. 131, n. 3, p. 912, doi. 10.1002/ange.201810130
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- Article
Structure and Reactivity of Al−O(H)−Al Moieties in Siloxide Frameworks: Solution and Gas‐Phase Model Studies.
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- Angewandte Chemie International Edition, 2019, v. 58, n. 3, p. 902, doi. 10.1002/anie.201810130
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- Article
Mapping and classifying molecules from a high-throughput structural database.
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- Journal of Cheminformatics, 2017, v. 9, n. 1, p. 1, doi. 10.1186/s13321-017-0192-4
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- Article
How Cations Change Peptide Structure.
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- Chemistry - A European Journal, 2013, v. 19, n. 34, p. 11224, doi. 10.1002/chem.201204554
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- Article
Ab initio MO Theory - An Important Tool in Foldamer Research: Prediction of Helices in Oligomers of ω-Amino Acids.
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- Helvetica Chimica Acta, 2012, v. 95, n. 12, p. 2348, doi. 10.1002/hlca.201200436
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- Article
A systematic study of fundamentals in α-helical coiled coil mimicry by alternating sequences of β- and γ-amino acids.
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- Amino Acids, 2011, v. 41, n. 3, p. 733, doi. 10.1007/s00726-011-0941-z
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- Article
A β/γ Motif to Mimic α-Helical Turns in Proteins.
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- ChemBioChem, 2010, v. 11, n. 3, p. 335, doi. 10.1002/cbic.200900700
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- Article
Synthesis and Structure of α/δ-Hybrid Peptides-Access to Novel Helix Patterns in Foldamers.
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- Chemistry - A European Journal, 2009, v. 15, n. 22, p. 5552, doi. 10.1002/chem.200802078
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- Article
Amide-to-Ester Substitution in Coiled Coils: The Effect of Removing Hydrogen Bonds on Protein Structure.
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- Angewandte Chemie International Edition, 2007, v. 46, n. 41, p. 7766, doi. 10.1002/anie.200702218
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- Article
Theoretical prediction of the basic helix types in α,β-hybrid peptides.
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- Biopolymers, 2006, v. 84, n. 4, p. 408, doi. 10.1002/bip.20493
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- Article
Side-chain control of folding of the homologous α-, β-, and γ-peptides into 'mixed' helices (β-helices).
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- Biopolymers, 2005, v. 80, n. 5, p. 675, doi. 10.1002/bip.20249
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Gemischte Helices ein allgemeines Faltungsmuster in homologen Peptiden? ( Diese Arbeit wurde unterstützt durch die Deutsche Forschungsgemeinschaft (Projekt HO2346/1 Sekundärstrukturbildung in Peptiden mit nichtproteinogenen Aminosäuren und SFB 610 Proteinzustände mit zellbiologischer und medizinischer Relevanz) und den Fonds der Chemischen Industrie. )
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- Angewandte Chemie, 2004, v. 116, n. 12, p. 1621, doi. 10.1002/ange.200353249
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- Article
Mixed HelicesA General Folding Pattern in Homologous Peptides? ( This work was supported by the Deutsche Forschungsgemeinschaft (Project HO2346/1 Sekundärstrukturbildung in Peptiden mit nicht-proteinogenen Aminosäuren and SFB 610 Proteinzustände mit zellbiologischer und medizinischer Relevanz) and the Fonds der Chemischen Industrie. )
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- Angewandte Chemie International Edition, 2004, v. 43, n. 12, p. 1594, doi. 10.1002/anie.200353249
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- Article