Phi-Value and NMR Structural Analysis of a Coupled Native-State Prolyl Isomerization and Conformational Protein Folding Process

Phi-Value and NMR Structural Analysis of a Coupled Native-State Prolyl Isomerization and Conformational Protein Folding Process

Prolyl <i>cis</i>/<i>trans</i> isomerization is a rate-limiting step in protein folding, often coupling directly to the acquisition of native structure. Here, we investigated the interplay between folding and prolyl isomerization in the N2 domain of the gene-3-protein from fi...

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Bibliographic Details
Main Authors: Ulrich Weininger, Maximilian von Delbrück, Franz X. Schmid, Roman P. Jakob
Format: Article
Language:English
Published: MDPI AG 2025-02-01
Series:Biomolecules
Subjects:
protein folding
prolyl isomerization
NMR spectroscopy
Phi-value analysis
protein stability
Online Access:https://www.mdpi.com/2218-273X/15/2/259
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