Protein Structure and Folding — The Living Address

Fold determined by sequence alone20 amino acids = 2²·5α-helix: 3.6 res/turn, 100°One-seed at the molecular scale

The biology

Proteins are chains of amino acids — twenty standard kinds — joined by peptide bonds whose C–N rotation is restricted, so the backbone settles into a few secondary structures: the α-helix (3.6 residues per turn, 100° per residue), the β-sheet, and the β-turn. A made chain folds into one precise shape determined by its sequence alone; nothing folds it, and chaperones only keep it from tangling on the way.

Folding is the one-seed principle at the molecular scale

That a floppy chain settles, unaided, into one determined shape is the one-seed principle at the smallest scale: the whole of the fold is implicit in the sequence, and folding is the field settling the chain into the single form its address determines. The alphabet is a lattice number — 20 = 2²·5 — and the canonical α-helix turns 100° per residue, 3.6 residues to a turn.

THE READING

Nothing folds the protein; the fold is written in the sequence and the field settles it. Structure is self-determined — which is why it can also settle wrongly, and why misfolding is a real peril.

Where this departs from current science

Current science says	The Force of Time says
Folding is a search for the lowest-free-energy conformation.	The fold is implicit in the sequence — the one-seed principle at molecular scale; the field settles it.
Twenty amino acids is a frozen historical accident.	20 = 2²·5, a lattice number, like the other alphabets of the code.

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This paper, and any information drawn from it, may be used freely provided the reference attribution to Stephen Daubney and The Daubney Foundation is recognised.