Protein folding

Protein folding is the process by which an amino-acid chain adopts a three-dimensional structure. That structure enables the protein’s biological function.

Protein structure: The arrangement of atoms in a protein, described at primary, secondary, tertiary, and quaternary levels. Folding creates the higher-order structures within this hierarchy.
Amino acid: An organic molecule with amino and carboxyl groups; amino acids are the building blocks of proteins. Each amino acid contributes a side chain that affects folding.
Protein structure prediction: The computational or experimental determination of a protein’s three-dimensional structure from available data, often its sequence. Prediction methods aim to infer the folded structure from sequence and other evidence.
Protein misfolding: The adoption of a protein structure that differs from its functional native state. It is the failure mode against which successful folding is defined.
Levinthal's paradox: The observation that exhaustive sampling of a protein’s possible conformations would take far longer than observed folding times. It poses the puzzle of how proteins find their structures so quickly.
Anfinsen's dogma: The principle that a protein’s amino-acid sequence contains the information needed to determine its native structure under suitable conditions. It connects a protein’s sequence to its folded structure.
Peptide bond: The covalent amide bond linking amino acids in a protein chain. Its restricted geometry limits the chain’s possible conformations.
AlphaFold: A deep-learning system developed by DeepMind for predicting protein structures from amino-acid sequences and related data. It produced highly accurate structural predictions for many proteins.
Protein aggregation: The accumulation of proteins into assemblies through interactions between protein molecules. Misfolded proteins can expose surfaces that promote aggregation.
Protein folding kinetics: The study of the rates and pathways by which proteins move from unfolded to folded states. Different proteins reach their folded states through distinct pathways and timescales.

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