A Closer Look at Type I Left‐Handed β‐Helices Provides a Better Understanding in Their Sequence–Structure Relationship: Toward Their Rational Design
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| Format: | Artículo Open Access |
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2024
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| _version_ | 1867004847241297920 |
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| author | Maxime Naudé Peter Faller Vincent Lebrun |
| author_facet | Maxime Naudé Peter Faller Vincent Lebrun Maxime Naudé Peter Faller Vincent Lebrun |
| collection | Wiley Open Access |
| contents | A Closer Look at Type I Left‐Handed β‐Helices Provides a Better Understanding in Their Sequence–Structure Relationship: Toward Their Rational Design Maxime Naudé Peter Faller Vincent Lebrun Proteins: Structure, Function, and Bioinformatics ABSTRACT Understanding the sequence–structure relationship in protein is of fundamental interest, but has practical applications such as the rational design of peptides and proteins. This relationship in the Type I left‐handed β‐helix containing proteins is updated and revisited in this study. Analyzing the available experimental structures in the Protein Data Bank, we could describe, further in detail, the structural features that are important for the stability of this fold, as well as its nucleation and termination. This study is meant to complete previous work, as it provides a separate analysis of the N‐terminal and C‐terminal rungs of the helix. Particular sequence motifs of these rungs are described along with the structural element they form. 10.1002/prot.26726 http://creativecommons.org/licenses/by-nc-nd/4.0/ |
| doi_str_mv | 10.1002/prot.26726 |
| format | Artículo Open Access |
| id | wiley_oa_10_1002_prot_26726 |
| institution | Wiley Open Access |
| license_str_mv | http://creativecommons.org/licenses/by-nc-nd/4.0/ |
| publishDate | 2024 |
| publisher | Wiley |
| record_format | wiley_oa |
| spellingShingle | A Closer Look at Type I Left‐Handed β‐Helices Provides a Better Understanding in Their Sequence–Structure Relationship: Toward Their Rational Design Maxime Naudé Peter Faller Vincent Lebrun Proteins: Structure, Function, and Bioinformatics A Closer Look at Type I Left‐Handed β‐Helices Provides a Better Understanding in Their Sequence–Structure Relationship: Toward Their Rational Design Maxime Naudé Peter Faller Vincent Lebrun Proteins: Structure, Function, and Bioinformatics ABSTRACT Understanding the sequence–structure relationship in protein is of fundamental interest, but has practical applications such as the rational design of peptides and proteins. This relationship in the Type I left‐handed β‐helix containing proteins is updated and revisited in this study. Analyzing the available experimental structures in the Protein Data Bank, we could describe, further in detail, the structural features that are important for the stability of this fold, as well as its nucleation and termination. This study is meant to complete previous work, as it provides a separate analysis of the N‐terminal and C‐terminal rungs of the helix. Particular sequence motifs of these rungs are described along with the structural element they form. 10.1002/prot.26726 http://creativecommons.org/licenses/by-nc-nd/4.0/ |
| title | A Closer Look at Type I Left‐Handed β‐Helices Provides a Better Understanding in Their Sequence–Structure Relationship: Toward Their Rational Design |
| topic | Proteins: Structure, Function, and Bioinformatics |
| url | https://onlinelibrary.wiley.com/doi/10.1002/prot.26726 |