The mechanism by which a linear sequence of amino acids controls the folding of a protein into its unique three-dimensional structure remains incompletely understood. In April 8 online Nature Structural Biology, Christian Wigley and colleagues from University of Texas Southwestern Medical Center, Dallas, show that a protein sequence can encode the native structure by disfavouring the formation of a misfolded structure.Wigley et al. observed that a proline residue in the center of the third trans
The mechanism by which a linear sequence of amino acids controls the folding of a protein into its unique three-dimensional structure remains incompletely understood. In April 8 online
Wigley
"Incorporation by nature of such 'negative folding determinants', aimed at preventing the formation of off-pathway structures, represents an additional mechanism by which folding information is encoded within the evolved sequences of proteins", concluded the ...
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