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Updated: May 29, 2025

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
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Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

2.9K

プロリンcis/トランス 適合性選択制御 14-3-3 拘束力

Frederik F Theisen1,2, Andreas Prestel1, Nina L Jacobsen1

  • 1Structural Biology and NMR Laboratory, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, Copenhagen DK-2200, Denmark.

Journal of the American Chemical Society
|February 5, 2025
PubMed
まとめ

本質的に無秩序なタンパク質領域 (IDR) でのプロリンイソメリゼーションは,異なるタンパク質の形を作り出します. この研究は,プロリン同位体特異的な14-3-3タンパク質への結合を明らかにし,細胞シグナル伝達に影響を与えています.

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Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

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Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins11:34

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

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Covalently Linked Protein Regulators02:04

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Ligand Binding and Linkage

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Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
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