ReviewFrontiers in molecular biosciences2022
AlphaFold 2 and NMR Spectroscopy: Partners to Understand Protein Structure, Dynamics and Function.
Review in Frontiers in molecular biosciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
- AI Designed Conformation Locking Peptides Target STING to Restore Diabetic Wound Healing.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Navigating the uncharted: AI-driven advances in protein structure, dynamics, interactions and ligand interactions for understudied families.BioData mining · 2026Review
- AI in Drug Discovery: Clinical Failures, Regulatory Reality, and the Validation Crisis Behind the Hype.Pharmaceuticals (Basel, Switzerland) · 2026Review
- Bridging structure and function: artificial intelligence-based modelling of kidney proteins.Nature reviews. Nephrology · 2026Review
- Shoebill: an interpretable AlphaFold2-informed predictor of protein crystallization propensity using XGBoost.Briefings in bioinformatics · 2026Article
- Article
- Comparative evaluation of the prediction accuracy of AlphaFold and ESMFold for monomeric and dimeric proteins.NAR genomics and bioinformatics · 2026Article
- Modernizing biomolecular NMR: The POKY suite.The Journal of biological chemistry · 2026Review
- Chimeric Approach to Identify Molecular Determinants of Nicotinic Acetylcholine Receptors.International journal of molecular sciences · 2026Review
- CASP16 Protein Monomer Structure Prediction Assessment.Proteins · 2026Article
- The transformative impact of AI-enabled AlphaFold 3: evolution, current status, and future prospects in structural biology.Frontiers in artificial intelligence · 2026Review
- In silico pharmacological analysis of Tinospora cordifolia compounds targeting African swine fever virus B175L.PloS one · 2026Article
- The molecular complexity of deep vein thrombosis was preliminarily explored based on the ceRNA network, scRNA-seq and AlphaFold 2.BMC medical genomics · 2025Article
- Hidden protein disorder: Deciphering the structural organisation and dynamics of a non-canonical CP12 from the diatom Thalassiosira pseudonana.The FEBS journal · 2025Article
- Deep learning in next-generation vaccine development for infectious diseases.Molecular therapy. Nucleic acids · 2025Review
- Resurgence of magnetic resonance techniques in the era of AlphaFold.Biophysical reviews · 2025Review
- Protein aggregation and neurodegenerative disease: Structural outlook for the novel therapeutics.Proteins · 2025Review
- Article
- Molecular mechanisms and consequences of TDP-43 phosphorylation in neurodegeneration.Molecular neurodegeneration · 2025Review
- To be, or not to be cleaved: Directed evolution of a canonical serine protease inhibitor against active and inactive protease pair identifies binding loop residue critical for prevention of proteolytic cleavage.Protein science : a publication of the Protein Society · 2025Article
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Authors and funding
1 author.
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Abstract
The artificial intelligence program AlphaFold 2 is revolutionizing the field of protein structure determination as it accurately predicts the 3D structure of two thirds of the human proteome. Its predictions can be used directly as structural models or indirectly as aids for experimental structure determination using X-ray crystallography, CryoEM or NMR spectroscopy. Nevertheless, AlphaFold 2 can neither afford insight into how proteins fold, nor can it determine protein stability or dynamics. Rare folds or minor alternative conformations are also not predicted by AlphaFold 2 and the program does not forecast the impact of post translational modifications, mutations or ligand binding. The remaining third of human proteome which is poorly predicted largely corresponds to intrinsically disordered regions of proteins. Key to regulation and signaling networks, these disordered regions often form biomolecular condensates or amyloids. Fortunately, the limitations of AlphaFold 2 are largely complemented by NMR spectroscopy. This experimental approach provides information on protein folding and dynamics as well as biomolecular condensates and amyloids and their modulation by experimental conditions, small molecules, post translational modifications, mutations, flanking sequence, interactions with other proteins, RNA and virus. Together, NMR spectroscopy and AlphaFold 2 can collaborate to advance our comprehension of proteins.
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