AbstractA model of the protein backbone is considered in which each residue is characterized by the location of its Cα atom and one of a discrete set of conformal (ϕ, ψ) states. We investigate the key differences between a description that offers a locally precise fit to known backbone structures and one that provides a globally accurate fit to protein structures. Using a statistical scoring scheme and threading, a protein's local best‐fit conformation is highly recognizable, but its global structure cannot be directly determined from an amino acid sequence. The incorporation of information about the conformal states of neighboring residues along the chain allows one to accurately translate the local structure into a global structure. We present a two‐step algorithm, which recognizes up to 95% of the tested protein native‐state structures to within a 2.5 Å root mean square deviation. Proteins 2004;55:000–000. © 2004 Wiley‐Liss, Inc.