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).

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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
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article

Cover Feature: Backbone Modification in a Protein Hydrophobic Core (Chem. Eur. J. 45/2024)

W. Seth Horne, Yuhan Lin
Chemistry - A European Journal
Protein Structure and Dynamics
article

Cover Feature: Backbone Modification in a Protein Hydrophobic Core (Chem. Eur. J. 45/2024)

W. Seth Horne, Yuhan Lin
article en

Abstract

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).

Chemistry - A European JournalVol. 30(45)
University of Pittsburgh (US)
Openalex Percentile: Top 88%
Protein Structure and Dynamics
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