The forces that fold a protein

Two views of the same idea. The forces shows the actual hydrogen bonds, salt bridges, and hydrophobic core inside a real, experimentally-determined structure. The funnel shows why those forces let a chain find its shape without an impossible blind search.

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Contacts are computed live from the deposited coordinates with standard geometric cut-offs: hydrogen bonds as backbone N···O closer than 3.5 Å (residues ≥2 apart), salt bridges as acidic O (Asp/Glu) to basic N (Lys/Arg/His) closer than 4.0 Å — the two participating side chains are drawn as sticks and labelled, acidic (negative) in red and basic (positive) in blue, so you can see each bridge is a pair of nearby oppositely-charged side chains — disulfides as S–S closer than 2.5 Å. Structures from the PDB; viewer built with 3Dmol.js.