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This short communication introduces a novel method for identification of the folding cores in proteins. Positive and negative charge centers, defined solely from the structure of the folded protein are likely to indicate the protein's folding core. The residues and sequences, identified by the procedure, are highly consistent with the available biochemical data on folding as seen for a set of about 20 proteins. Here, the folding of chymotrypsin inhibitor-2 (CI2) from barley is analyzed in some detail.

Identification of Protein Folding Cores Using Charge Center Model of Protein Structure