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...

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Bibliographic Details
Published in:	Journal of molecular biology Vol. 437; no. 2; p. 168900
Main Authors:	Gavalda-Garcia, Jose, Dixit, Bhawna, Díaz, Adrián, Ghysels, An, Vranken, Wim
Format:	Journal Article
Language:	English
Published:	Netherlands Elsevier Ltd 15.01.2025
Subjects:	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 Access:	Get full text
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