Backbone Modification in a Protein Hydrophobic Core
Abstract: Targeted protein backbone modification can recreate tertiary structures reminiscent of folds found in nature on artificial scaffolds with improved biostability. Incorporation of altered monomers in such entities is typically limited to sites distant from the hydrophobic core to avoid potential disruptions to folding. This is limiting, as it is advantageous in some applications to incorporate artificial connectivity at buried sites. Here, we report an examination of protein backbone modification targeted specifically to hydrophobic core positions and its impacts on tertiary folded structure and fold stability. Different artificial monomer types are placed at core, core‐flanking, or solvent‐exposed positions in a compact three‐helix protein. Effects on structure and folding energetics are assessed by NMR spectroscopy and biophysical methods. Results show that artificial residues can be well accommodated in the hydrophobic core of a defined tertiary fold, with effects on stability only modestly larger than identical changes at solvent‐exposed sites. Collectively, these results provide new insights into folding behavior of protein‐like artificial chains as well as strategies for the design of such molecules.
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Erschienen in
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Backbone Modification in a Protein Hydrophobic Core ; day:24 ; month:06 ; year:2024 ; extent:8
Chemistry - a European journal ; (24.06.2024) (gesamt 8)
- Urheber
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Lin, Yuhan
Horne, W. Seth
- DOI
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10.1002/chem.202401890
- URN
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urn:nbn:de:101:1-2406251414565.618167022599
- Rechteinformation
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
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14.08.2025, 10:46 MESZ
Datenpartner
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Lin, Yuhan
- Horne, W. Seth
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