Gradations in protein dynamics captured by experimental NMR are not well represented by AlphaFold2 models and other computational metrics

[Display omitted] •AlphaFold2’s pLDDT can differentiate between ordered or disordered residues.•AlphaFold2’s pLDDT does not reflect gradations on residue dynamics.•Biases in the training sets result in predicted rigidity of flexible regions.•Conformational diversity in NMR ensembles is associated wi...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Journal of molecular biology Jg. 437; H. 2; S. 168900
Hauptverfasser:	Gavalda-Garcia, Jose, Dixit, Bhawna, Díaz, Adrián, Ghysels, An, Vranken, Wim
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	Netherlands Elsevier Ltd 15.01.2025
Schlagworte:	AlphaFold2 Computational Biology - methods large-scale analysis Magnetic Resonance Spectroscopy - methods Molecular Dynamics Simulation nuclear magnetic resonance Nuclear Magnetic Resonance, Biomolecular - methods Protein Conformation protein dynamics Protein Folding Proteins - chemistry structural biology structural biology nuclear magnetic resonance large-scale analysis protein dynamics AlphaFold2
ISSN:	0022-2836, 1089-8638, 1089-8638
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!