1 Department of Biomolecular Structural Chemistry, Max F. Perutz Laboratories, Vienna University, Campus Vienna Biocenter 5, A-1030 Vienna, Austria
2 Department of General Chemistry, Pavia University, Viale Taramelli 12, I-27100 Pavia, Italy
Predictions of protein conformational disorder are important in structural biology since they can allow the elimination of protein constructs, the three-dimensional structure of which cannot be determined since they are natively unfolded. Here a new procedure is presented that allows one to predict with high accuracy disordered residues on the basis of protein sequences. It makes use of twelve prediction methods and merges their results by using least-squares optimization. A statistical survey of the Protein Data Bank is also reported, in order to know how many residues can be disordered in proteins that were crystallized and the three-dimensional structure of which was determined.
Received Date: 12/11/2007 Revision Received Date: 26/11/2007 Acceptance Date: 12/12/2007 Electronic publication date: 18/1/2008 Collection year: 2008
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