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One popular model for protein folding, the framework model, postulates initial formation of secondary structure elements, which then assemble into the native conformation. However, short peptides that correspond to secondary structure elements in proteins are often only marginally stable in isolation. A 33-residue peptide ( G C N C p l ) corresponding to the GCN4 leucine zipper folds as a parallel, two- Deletion of the first residue (Arg 1) results in local, N-terminal unfolding of the coileddoi:10.1021/bi00189a042 pmid:8003501 fatcat:bkc5nrpldbf7fihpk3l6sli7eq