Intrinsic protein disorder and conditional folding in <scp>AlphaFoldDB</scp>
Damiano Piovesan, Alexander Miguel Monzón, Silvio C. E. Tosatto
Abstract
Intrinsically disordered regions (IDRs) defying the traditional protein structure-function paradigm have been difficult to analyze. The availability of accurate structure predictions on a large scale in AlphaFoldDB offers a fresh perspective on IDR prediction. Here, we establish three baselines for IDR prediction from AlphaFoldDB models based on the recent CAID dataset. Surprisingly, AlphaFoldDB is highly competitive for predicting both IDRs and conditionally folded binding regions, demonstrating the plasticity of the disorder to structure continuum.
Topics & Concepts
Protein foldingIntrinsically disordered proteinsPerspective (graphical)Structure functionFunction (biology)Computer scienceFolding (DSP implementation)Protein structure predictionComputational biologyProtein structureStatistical physicsChemistryPhysicsBiologyArtificial intelligenceBiophysicsEvolutionary biologyBiochemistryEngineeringElectrical engineeringParticle physicsProtein Structure and DynamicsEnzyme Structure and FunctionMass Spectrometry Techniques and Applications