Cover Feature: Backbone Modification in a Protein Hydrophobic Core (Chem. Eur. J. 45/2024)
The hydrophobic core of a protein, made up of side chains buried away from water in the folded state, is a crucial element of protein structure. New results show that artificial backbone connectivity can be accommodated in the core of a tertiary fold with minimal impact on folded structure or stability. More information can be found in the Research Article by Y. Lin and W. S. Horne (DOI: 10.1002/chem.202401890).
Authors
- W. Seth Horne (ORCID: https://orcid.org/0000-0003-2927-1739)
- Yuhan Lin (ORCID: https://orcid.org/0000-0001-9065-1162)
Institutions
- University of Pittsburgh (US)
Publication Details
- Journal
- Chemistry - A European Journal
- Published
- 2024-08-12
- DOI
- https://doi.org/10.1002/chem.202484503
- Primary Topic
- Protein Structure and Dynamics
- Type
- article
- Field-Weighted Citation Impact
- 0.00