Linked from

The 50 pages that link to Protein folding, each with the reason it gives.

• Amino acidRelated: Amino-acid sequence and side-chain interactions guide the chain's final shape.

• EnzymeRelated: An enzyme's folded structure establishes the geometry of its active site.

• ProteinRelated: Folding creates the shapes that make many protein functions possible.

• Molecular dynamicsRelated: Simulations probe folding motions and the stability of candidate protein structures.

• Van der Waals forceRelated: Close packing of atoms lets van der Waals contacts help stabilize folded protein interiors.

• Protein structureRelated: It describes how a sequence acquires the arrangement represented by protein structure.

• Hydrophobic effectRelated: Burial of nonpolar residues is a major contribution to folding stability.

• Conformational isomerismRelated: Rotation around backbone bonds gives proteins many conformations along folding pathways.

• Translation (biology)Related: Newly translated chains must fold, often while synthesis is still underway.

• Optical rotationRelated: Optical rotatory dispersion can reveal changes in protein secondary structure.

• CysteineRelated: Cysteine disulfide bonds can constrain folding and stabilize the resulting structure.

• HydrophobicityRelated: Hydrophobic residues tend to become buried away from water in many soluble proteins.

• Protein engineeringRelated: Engineered sequences must fold into structures that support their intended functions.

• Circular dichroismRelated: Circular dichroism tracks structural changes during folding and unfolding.

• ConformationRelated: Folding selects a functional arrangement from many possible conformations.

• Protein crystallographyRelated: The folded structure is the object that crystallographic measurements aim to reveal.

• Structural biologyRelated: Folding links a protein’s sequence to the structures measured by the field.

• Torsional strainRelated: Backbone torsional energies help constrain the conformations available to a protein chain.

• BiosimilarRelated: Small structural variations can affect a biological medicine’s properties.

• Noncovalent interactionRelated: Hydrogen bonds, dispersion, ionic attractions, and hydrophobic effects collectively stabilize folded structures.

• Recombinant proteinRelated: A newly synthesized chain must fold into a structure that supports its activity.

• ThermophileRelated: Thermophile proteins must fold into structures that remain functional at high temperatures.

• Enzyme engineeringRelated: Engineered sequence changes can improve or disrupt folding and stability.

• Green fluorescent proteinRelated: GFP’s barrel-shaped fold protects the chromophore and enables fluorescence.

• Supramolecular chemistryRelated: Protein folding is a biological example of structure emerging from many noncovalent interactions.

• BiomoleculeRelated: A protein’s folded shape helps determine its activity and interactions.

• John KendrewRelated: Myoglobin’s solved structure gave researchers a concrete basis for investigating how proteins fold.

• ProlineRelated: Proline’s restricted geometry and slow bond isomerization can shape folding pathways.

• CystineRelated: Cystine bridges between protein cysteines can stabilize folded structures.

• Martin ChalfieRelated: GFP must fold correctly to form its fluorescent chromophore.

• Protein designRelated: A designed sequence must fold into the structure that supports its intended behavior.

• SulfolobusRelated: High-temperature growth makes stable folding and protein quality control essential in Sulfolobus.

• HydrophobicityRelated: Hydrophobic side chains often pack into protein interiors during folding in water.

• Michael LevittRelated: Levitt developed early computer simulations to investigate how protein structures form.

• Biomimetic nanotechnologyRelated: Protein shape and folding show how molecular structure can encode nanoscale function.

• Conformation & topologyRelated: Folding converts a sequence of connected residues into a specific conformation.

• G. N. RamachandranRelated: Allowed backbone conformations constrain the shapes available during folding.

• Ribbon diagramRelated: Ribbon views help communicate the folded shape and arrangement of secondary structures.